Abstract
Animal proteins from meat and its stuffs have recently been one of main concerns in the drive for sustainable food production. This viewpoint suggests that there are exciting prospects to reformulate meat products that are produced more sustainably and may also have health benefits by substituting high-protein nonmeat ingredients for some of the meat. Considering these pre-existing conditions, this review critically reviews recent data on extenders from several sources, including pulses, plant-based components, plant byproducts, and unconventional sources. We used the related keywords from Scopus-database without limiting the publishing date. With an emphasis on how these findings may impact the sustainability of meat products, it sees them as a great chance to enhance the functional quality and technological profile of meat. Therefore, to promote sustainability, meat alternatives such as plant-based meat equivalents are being made available. To boost consumer acceptability of these goods, further initiatives should also be developed to enhance the functioning of these innovative food items and increase public knowledge of plant-based meat analogues.
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Introduction
Meat is recognized as a very popular food item worldwide and it is well known as an excellent quality protein source with other nutritional characteristics along with its appealing taste. With the growing rate of the planet's population, the need for food security is rising as well, and to feed this growing population a greater amount of good quality food having proper protein, fat, and other nutrition is required. Meanwhile, increased environmental footprint awareness plays a significant role in meat analogues supply for the sustainable and transparent food security of the planet. Animal is the solitary bioresource of meat protein and with rapid population growth, the need for meat protein is also increasing. Various data show that the demand will be magnified near to twice by 2050 [1]. To cater to this high meat protein demand, more animal husbandry is required, but the scarcity of land, water, and other environmental factors constrain the growth of animal husbandry due to which meat price indices are continuously increasing, which makes it difficult in the adequate meat accessibility to the people of lower and lower-middle class group countries (Fig. 1). One of the major environmental concerns is also emission of greenhouse gases (carbon dioxide (CO2), methane (CH4) and nitrous oxide (N2O)) from livestock farming (Fig. 2). In the search for an alternative to conventional animal-derived meat protein, nowadays search for alternative protein has become very common, where plant-based meat analogues (PBMA) emerge as the most popular alternative [2]. Meat analogues are generally mock meat substitutes or imitation meat having all the structural and nutritional characteristics of meat along with the aesthetic qualities of specific types of meats [3]. The PBMA seems to be a wholesome solution to cater to all the following issues raised by animal meat such as high pricing of meat protein, religious concerns (halal/jhatka), greenhouse gas emissions from animal husbandry farms, and loss of biodiversity due to higher animal husbandry [4]. As people are becoming more aware of the importance of their health and environment, they are inclined to the PBMA [5]. Over a long period, scientists and researchers investigated different protein texturizing techniques to convert different plant-based proteins into meat analogues. The first attempt at texturing plant protein into meat analogues was made with soy protein isolate in 1970 where isolated soy protein was added to increase the protein level and enhance the texture of meatball, wiener, and hamburger compositions [3]. Nowadays to develop PBMA several protein sources like—soy protein, gluten, different legumes, vegetables, seeds, lentils, beans, peas, etc. are used as the main raw material. Plant-based proteins are converted to meat analogues mainly with the extrusion technology process and with time advancements in processing techniques resulting in mimic meats comprising enhanced nutritional qualities and functional meat-like characteristics [6, 7]. Based on moisture content PBMA is mainly two types—low moisture meat analogues that contain moisture content of less than 30% and high moisture content meat analogues that contain moisture content between 50 and 70% [8]. Low moisture content meat analogues are also known as texturized vegetable protein, and it is used with the combination of real meat to get a meat-like texture and qualities. High moisture content meat analogues are gaining rapid attention in the industries for their applicability as a whole meat substitute. In animal meat, one of the major concerns is high saturated fat content and high cholesterol content, which causes severe cardiovascular diseases and also other major problems such as hypertension, weight gain, etc. [9]. Different processed animal meat products like curing meat and smoking meat raised concerns about their possible carcinogenic phenomena [10]. PBMA—as a natural plant-based protein is a primary ingredient that imparts several vitamins, minerals, proteins, fibres, anti-oxidants, and polyphenols into our body system that keeps our body healthy [11]. In animal meat, there is a chance to transfer various animal-borne diseases into the body system through meat intake and this might cause serious illness in the human body, but the chances of similar issues from PBMA are low [2]. Nowadays from a healthy life point of view and different religious concerns, people are moving towards a vegan diet and for them, PBMA gives an excellent option to get meat-like taste, mouthfeel, and nutritional functionalities without meat intake.
Changes in the different meat prices as per FAO meat price index. (Data Source: OECD-FAO Agricultural Outlook 2022–2031)
Meat Greenhouse gas emissions intensity per region
This paper collects and synthetizes the available research on plant-based meat analogues. The Scopus database was used to retrieve the data. The Scopus database was searched for data in January 2023 using the following keywords: (plant proteins) AND (meat analogues OR meat alternatives OR meat formulation OR ingredients OR functionalities). The PRISMA guidelines (www.prisma-statement.org) were used for data refinement where the total number of primary searches was 806; after filtering the documents, the final number of relevant articles was 403. For this review, all titles, and abstracts of identified articles were screened by the authors and the full text was evaluated if appropriate. Additional inclusion criteria were that the article should deal specifically with meat analogues using plant proteins, not other sources. No temporal restrictions were applied to the literature search. Figure 3 reported the bibliometric analysis of plant protein-based meat analogues, data were captured from Scopus.
The bibliometric analysis of plant protein-based meat analogues
Meat analogues
Potential ingredients for meat analogues
Figures 4 and 5 portray the necessary ingredients needed for developing PBMA. The specific amount of all the ingredients with accurate formulation will result in the desired mock meat characteristics of the developed meat analogues.
Graphical representation of different ingredients used in PBMA preparation
Different ingredients and their functions used in PBMA-formulation
Plant proteins as promising ingredients
Proteins are made up of amino acids that are critical for human health and are mostly used in food processing to create a variety of nutritious diets [12]. Dietary proteins are the basic source of nitrogen, and amino acids serve as construction blocks for human tissue while also requiring physiological enzymes to regulate chemical and biological reactions for the body to function properly [13]. Plant-based proteins (PBP) have gained popularity recently because of the change in particular dietary habits that most people are adopting. There are several PBP, for instance, soy protein, legume-based protein, wheat gluten, and various seed proteins are used in PBMA-developing (Fig. 6). Soy protein is extensively used in PBMA-developing due to its low cost, easily available, and superior functionalities. The reason for the increased focus on PBP is a recently discovered link between the intake of animal protein products and an enlarged hazard of chronic diseases [14]. Another reason for the increased prominence of PBP is the environmental issues caused by livestock agriculture. Recently, PBP was used as meat analogues in local and international markets. The global market for meat substitutes was $4,532.6 M in 2019 and is expected to reach $7,106.7 M in 2025. Between 2020 and 2025, this is with an estimated CAGR of 7.7%. Market trends and category development are influenced by regional variations; with 70% each, Europe and North America dominated the global market in 2019. Additionally, Asia Pacific held a significant share and is anticipated to grow at the fastest CAGR. The Middle East and Africa have a small share of the market, so they could be underexplored.
Classification of different types of protein used in the preparation of plant-based meat analogues
Usage of soy protein for meat analogues
Soybeans are rich in protein and contain water-soluble and insoluble proteins. Based on the dry weight of mature raw seeds, soybeans have ~ 8.5–13% moisture, ~ 33–40% protein, ~ 3–4% ash, ~ 18–20% fats, and ~ 9–12% fibers [15]. The variation in protein content may be due to cultivation environments, variety, and genetic modification. Soy protein has been utilized to create fabricated soy products, including soy protein isolates, soy protein concentrates, and soy-deflated flour [16]. Based on their sedimentation coefficients (pH 4.5–4.8), the extractable globular proteins are divided into four categories: 2S, 7S, 11S, and 15S [17]. For instance, it was discovered that 7S-rich soy protein gels produced at pH 3 had greater strain at breakup and greater water-holding capability as compared to 11S-rich gels [18, 19]. Soybeans have good protein quality, so their food products are amazing plant-based protein sources [20]. Kumar and his co-workers reported that because of the proportionate nutritional content of soybeans, it is being used to substitute red meat [21]. On the level of Protein Digestibility Corrected Amino Acid Score, soybean protein received the highest possible score of 1.0 for being equivalent to animal [22]. The meat analogues are made from a combination of non-textured and textured soy proteins [23]. Soy proteins were utilized to make various products, including chicken-style nuggets and breasts, meat-free sausages, and sliced cooked meats [22]. Patterned soy protein concentrates resemble the fibres of meat muscle, such as those found in chicken breast meat [24]; provide meat-like fibrous qualities such as mouth feel, chewiness, and hardness [25]. Due to the creation of new technologies that have made processes more efficient, the production of plant proteins has gained popularity over the past decade [26]. As one of the most widely used alternatives to cow milk, soy milk is a typical product made with soy protein. Diverse processing technologies are utilized to create a kind of other products, embracing tofu, meals, soy sauce, and soy oil. To avoid overheating, which results in protein denaturation, non-thermal processing methods like fermentation and protein isolation/concentration are utilized in the creation of soy protein products [27]. The protein content and essential amino acids are shown in Table 1 [35,36,37]. Meanwhile, Table 2 lists literature on the functional properties along with the application perspective of diverse soy ingredients, and further protein-rich constituents. After processing like toasting or moisture cooking or even mixing with other proteins or polysaccharides is recommended for tweaking the protein possessions [28,29,30]. For meat analog uses, the protein concentration need not to be greater. The robust combinations of soy protein isolate (SPI) and gluten or soy protein concentrates (SPC) were employed to produce TVP-based patties, whereas lower refined constituents were also employed for soy emulsions and gels for sausages, or for structuring muscle-like products [1, 31,32,33,34].
Usage of gluten protein for meat analogues
Wheat gluten is a significant component of many analogues. Because it is a by-product of the creation of colossal wheat starch, its price is appealing to the industry. In contrast to soy, the insoluble protein is left behind after the soluble and dispersible components of wheat are only removed by washing them with water [38]. In addition to its ability to bind and form the dough, wheat gluten has other desirable properties like viscosity, swelling, and nutritional quality [39]. The protein content of vigorous wheat gluten and extracted wheat gluten ranges from 75 to 80% and 90%, respectively. While globulins make up most pulse proteins, gliadin and glutenin, which make up 85% of the proteins, make wheat gluten proteins stand out from other plant proteins due to their extremely distinctive properties [34, 40]. Upon simple deformation and elongation, gluten forms thin protein films, converting the meat-like dough into a fibrous substance [32]. The linking of disulfide proteins results in this three-dimensional network, which also leads to the creation of fibrous structures during rise-moisture extrusion [41, 42].
Gliadin (prolamin) is soluble in alcohol, whereas glutenin (glutelin) is soluble in diluted acid [43]. When gliadin and glutenin are combined into water, they form a complex that gives rise to the viscoelastic matrix found in bread dough. They make disulfide linkages, which form the fibrous structure found in textured plant proteins [44]. Gliadin is responsible for the flow of wheat dough, while glutenin is responsible for its elasticity and strength [43]. To achieve the anticipated viscoelastic things and product characteristics, the ratio of these two wheat constituents is crucial [45]. Through the treatment and extrusion processes, wheat protein can replicate the texture of meat thanks to the viscoelastic and economical properties of wheat gluten. Consequently, among all other cereals, wheat gluten is specifically comprised in the construction of meat analogues [1]. Products made with wheat gluten can contain the components of textured vegetable protein. These elements could be utilized as meat extenders and meat analogues. For example, in-ground meat patties' gluten can be used as a binder and protracted to create reordered products. In addition, hydrated gluten can be transformed into fibers via an extrusion and texturizing process into a variety of meat substitutes [46].
Usage of legume protein for meat analogues
Globally, 27% of the beans and pulses in the Leguminosae family are produced as primary crops. Protein is abundant in a diet rich in legumes. The evaluation of various characteristics such as foam stabilization and gel formation of pulses namely chickpea, lupine, and lentil) as well as beans demonstrates that pea protein is the most appropriate for use in the formulation of meat analogues [47]. Researchers have successfully developed a meat analog made of pea protein, which resembles fish and chicken meat in its fibrous texture; that improved the product's hydration by including high moisture starch, 90% protein from pea protein isolates, and 80% protein from gluten. Legumes are an essential component of human nutrition because they contain a lot of protein, starch, fiber, and essential amino acids (such as arginine, lysine, glutamic acid, leucine, and aspartic acid) [48]. Proteins from unprocessed legumes are easier to digest than those from animal sources [49]. Due to their functional attributes, quality, texture, and economic significance, meat-based legumes are seeing a significant increase [50].
Additionally, the proteins of lupine, lentils, faba beans, mung beans, and chickpeas are capable of foam and emulsion stabilization [51]. Sadly, lentil, lupine, and faba bean proteins have lower gelling properties than soy proteins [52] On the other hand, mung beans and chickpeas have good gelling properties, making them more promising as meat substitutes [53]. Recent studies have primarily focused on comprehending and enhancing the functionality of components (mainly isolates). Under optimal treatment conditions, legume proteins' gelling properties and thermal stability have been enhanced by ultrasonication [54]. Vogelsang-O'Dwyer et al. [55] demonstrated that dry fractionated protein-rich faba bean flour outperformed isolate formed by acid extraction/isoelectric precipitation in terms of functionality. At pH 7, the earlier had greater protein solubility (85%), a greater capacity for foaming, and excellent gelling properties [55]. Consequently, many researchers investigate the features of legumes that have been slightly fractionated through milling and air classification [56].
Usage of seed protein for meat analogues
Oilseeds like rapeseed, canola, or sunflower recently have become cynosure along with soy and legumes. However, most seed isolates and concentrates are still not profitably accessible. These impart capabilities for substituting for soy in formulations of plant-based foods. The proteins extracted from by-products of the oil industry make their economic valorization very appealing. The existence of anti-nutritional parameters or polyphenols, which have the potential to interact with proteins and prevent their use in human nutrition, has led to limitations are currently dealt with extraction protocols and fermentation processes [57,58,59]. Salgado et al. [60] showed that sunflower protein concentrates, like commercial soy protein isolates employed in the form of a thickener, have reasonable water-holding ability [192]. In addition, sunflower proteins, like commercial soybean protein isolates and bovine serum albumin, are known to be stable in emulsions and foams. In addition, sunflower protein concentrates demonstrated a gelation ability to that of commercial proteins utilized in a variety of applications as gelling agents. When sunflower isolates were subjected to ultrasonic treatment at a temperature of 95 °C, stronger gels were produced. The firmness of the gels augmented with the temperature drop to 25 °C [61]. Like sunflower proteins, rapeseed proteins, which are mostly made up of cruciferin (11S globulin) and napin (1.7–2S albumin), can form gels when subjected to high pressure or heat, which may help produce textures that resemble those of meat [62]. However, it was stated that the characteristics of the rapeseed protein subunits differ; under alkaline conditions, cruciferin forms a strong heat-set gel, whereas napin generally forms a weaker gel [63]. Besides, it was found that protein extract of rapeseed usually forms gels at a pH of 7, but once these proteins are heated, they create gooey-like conduct at pH values of 5 and 7 [64]. According to many other literature studies, gelation of rapeseed and canola proteins characteristically encompasses the use of polysaccharide mixtures, chemical alteration of the proteins (such as succinylation and acetylation), and the addition of a fixative (such as transglutaminase) [65].
Pseudo-cereals like quinoa seeds have gained popularity as a source of protein as well. Whole seeds and flour, which are less refined quinoa ingredients, were utilized as meat extenders in nuggets in meat products, gelling in mortadella, and fat replacers in burgers [66,67,68]. At a neutral pH, quinoa isolate has a solubility of less than 50%, but its water absorption, emulsifying, and foaming characteristics are comparable to those of soy protein [69]. Except for low moisture extruded snacks, there have been few studies on the application of quinoa in extrusion processes so far. This suggests that TVP-based products and sausage-type products would benefit more from using quinoa protein as an ingredient.
The chia and pumpkin seed proteins are still being studied, so the emphasis is on protein purification (via alkaline pretreatment and dry separation) and the functionality that outcomes [70, 71]. The less refined fractions had the lowest emulsifying stability for chia protein-rich elements, whereas the dry fractionated protein-enriched fractions had the highest protein solubility, water absorption, foaming, and gelling capacity [72]. Their potential in the form of a constituent in emulsion-like products, namely sausages, is indicated by these properties. Like chia seed protein, pumpkin seed proteins have a relatively low solubility (less than 20%) in the acidic pH range (pH 5), but their solubility dramatically upsurges at a pH greater than 6 [73]. With unfolding temperatures > 90 °C, pumpkin seed protein appears to be more resistant than other proteins [70]. Further alteration should be taken into consideration because this can be the cause of these proteins' absence of crucial capabilities. Table 3 provides a summary of various plant protein-based BAP extractions, and Fig. 7 depicts its water and enzyme extraction.
Schematic diagram of enzyme-assisted protein extraction and protein water extraction
Usage of cereal proteins for meat analogues
Cereal protein includes various types of protein obtained from rice, wheat, oats, barley, etc. Cereal grain has more protein than legumes but less than soy protein. Among all the cereal proteins, wheat gluten is extensively used due to its low cost and excellent viscoelastic properties which makes it suitable to bind flavour, color, and other ingredients that result in the making of excellent meat analogues [39]. Along with an excellent swelling index wheat gluten provides both consistency and fiber-like texturing in the meat analogues. From a nutritional point of view, wheat gluten content has higher carbohydrate content and a poor amino acid profile where many essential amino acids are missing [86]. Wheat gluten has a very attractive low cost because it is obtained as a byproduct of wheat starch production. Disulfide protein linking and the ratio of glutenins and gliadins determines the gluten's ability to form a network-like 3-D texture formation [41]. It has been observed that other functional properties like foaming, emulsifying properties, and solubility of gluten were improved through hydrolysis [87].
Usage of other proteins for meat analogues
Besides all the above-discussed proteins, several other types of proteins are there such as—corn zein protein, peanuts, potato proteins, pumpkin, etc. can be used in the development of PBMA. Several research studies have already performed such as peanut flour being used in replace of soya flour, potato protein, and corn zein are blended to develop meat mimics the gel-like structure, but no clear results have been obtained till now [88]. The bottom-up design of proteins needed to develop meat analogues was imagined in Fig. 8.
The bottom-up design of proteins needed to develop meat analogues
Usage of lipids for meat analogues
Lipids have important functions in terms of providing the meat with juiciness, flavour release, and tenderness in the PBMA. Generally, meat analogues are developed from defatted protein sources that result in lesser fat content in the meat analogues. Therefore to increase the fat content minimally fractionated soy that contains higher fat is used in the manufacturing of fibrous structures like meat analogues [28]. Sometimes higher fat content (15% or higher) causes a high lubrication effect in the extrusion process and as a result, lower shear force is generated which badly affects the structural development of meat analogues [1]. In meat analogues, several types of fats and oils are used such as—sunflower oil, canola oil, rapeseed oil, coconut oil, soybean oil, corn oil, palm oil, etc. Oils help in the retention of volatile flavor components thus resulting in a good flavor profile in the meat analogues. From a nutritional point of view, oils with lower saturated fatty acids are preferred in meat analogues development. Vegetable oils are extensively used in meat analogues as they are cholesterol-free and contain higher unsaturated fatty acids. Nowadays oleo gels are used in the complete replacement of saturated fatty acids in many meat analogues products [89]. In recent times due to growing consumer awareness several fat substitutes such as dietary fibre, modified lipids, etc. have been used to develop low-fat meat analogues [44].
Usage of flavouring agents for meat analogues
In meat analogues, different flavour generation components and their critical interaction during processing have a crucial role in mimicking specific meat-like tastes and flavors. Meat analogue's taste and flavour predominate its acceptance as a meat alternative to the consumer. Uses of different spices, seasonings, herbs, sugars, salts, and savoury aromas, and their binding capacity to the plant proteins through the extrusion process are directly responsible for meat-like flavour generation [90]. Interaction of different sugars like glucose, fructose, and ribose with different amino acids such as methionine, lysine, and proline through milliard reaction generates characteristics meat-like flavor profile [91]. Unwanted off flavors generated by saponins, glycosides, catechins, and isoflavones in soy and legume protein are reduced by reducing fat content and deactivating lipoxygenases, which limit lipid oxidation [92]. The fatty acid content of various fats/oils used in meat analogues has a vital role in the production of the aromatic flavor profile of meat analogues. During the cooking process, the generation of new flavor components and retention of the volatile flavor components build the desired flavor and taste profile in the meat alternatives [93]. In a study, researchers reported the generation of beef and chicken-like flavor profile through enzymatic hydrolyses of plant-derived proteins [88]. Sulfur-containing compounds such as furan and thiophenes are directly responsible for the generation of a strong meat-like aroma and roast flavor in the meat alternatives [94].
Usage of colouring agents for meat analogues
In the consumer's opinion, color is the most important parameter to create a visual appeal for meat analogues in their mind. Each meat has some specific color that changes through different processes such as cooking and smoking. Similarly, meat analogues should have meat mimic color and color change characteristics during processing. Several heat colorings agents such as malt or annatto, turmin, leghemoglobin, erythrosine, cumin, caramel colors, carotene, canthaxanthin, and lycopene have been used to incorporate the meat color and color change characteristics in the meat analogues [46]. Specifically, to mimic the red color of meat leghemoglobin (beet juice extract) is used and to mimic the chicken color, titanium oxide is used in the meat analogues [4]. The colour-changing features of myoglobin during thermal processing in real meat are imitated in meat analogues by utilizing betanin and beetroot extracts, which create the same colour-changing behaviour during thermal processing [95]. During processing the main challenge is to protect the color compounds from thermal damage and for this ascorbic acids or juices like citrus fruit juice having high ascorbic acids are being used as a preservative to protect the color [96]. Through the Maillard reaction, reducing sugars such as xylose, maltose, etc. imparts a potent part in the final color formation of the meat analogues and the right composition of reducing sugars needs to be used in the formulation for specific final color generation in the meat analogues [97]. With growing consumer awareness, nowadays in PBMA more and more natural colourants are used which also possess anti-oxidant activities that encounter free radicals generated during thermal processing [98]. Several other factors such as pH, protein structure, extrusion parameters, amino acid composition, and flavoring ingredients also have an imperative part in the final color formation of the meat alternatives.
2.1.5. Usage of texturing and binding agents for meat analogues
Meat analogues are made by combining a variety of ingredients through different texturizing techniques. For optimum binding of all the necessary ingredients (flavor, color, stabilizers, emulsifier, thickeners) several binding and texturing agents such as different natural gums (xanthan gum, guar gum, locust bean gum), carrageenan, hydrocolloids (methylcellulose, hydroxypropyl methylcellulose), wheat gluten, soy protein concentrate, casein are used [99]. By retaining the optimum moisture and fat content different binding agents help to maintain juiciness, consistency, and smoothness in sausage-like meat analogues. It has been found that in emulsion-type products use of salt and phosphate enhances the binding capacity of myofibrillar proteins [100]. Protein quality and quantity have an important role in texturization. The higher the protein content, the higher the water holding and binding capacity resulting in a more juiciness-like texture. The adhesive characteristics of the ingredients used also improve the product's texture and binding capacity. Wheat gluten possesses superior binding quality and elastic properties [101]. In some non-vegan meat analogues, egg albumins are used as binding agents due to their adhesion characteristics and increase the overall protein content. Different hydrocolloids also provide a good binding capacity for vegetable protein with less oil absorption [102].
Usage of water for meat analogues
In meat analogues, water is a multi-functional ingredient, primarily from providing a hydration effect to the critical conformational change in protein water plays a crucial part in the designing of PBMA. In the extrusion process, high moisture content promotes greater hydrophobic interaction and the creation of disulfide bonds, and H-bonds [103]. The presence of water in meat analogues influences several functional qualities such as swelling index, gelling capacity, foaming capacity, viscosity, and emulsifying capabilities. In the sausage type of product, water plays a vital role in providing juiciness and mouthfeel [104].
Various formulations for meat analogues
Nowadays PBMA is gaining attention worldwide. Several studies reported different formulation compositions (Table 4, Fig. 9) with different ingredients and the outcomes helped to develop superior-quality meat analogues. Here in this section some of the recent studies are reported and their outcomes are analyzed. Chiang et al. [25] utilized a mixture of soy protein concentrate and wheat gluten in three different ratios along with the incorporation of vegetable oil as the fat source, pumpkin powder, wheat starch, and salt at a final protein concentration of 59.30% and observed that H-bond linked fibrous textured meat analogues were formed through extrusion process with optimum hardness and chewiness [25]. Krintiras et al. [105] utilized soy protein isolate and wheat gluten with a ratio of 3.3:1 along with 1% NaCl and observed that 30 mm thick highly fibrous textured meat analogues. Dekkers et al. [106] used a blend of pectin and soy protein isolate with the addition of NaCl and as a result elongated fibrous filament-like texture formed that is suitable for the designing of meat analogues. Dekkers et al. [107] employed a blend of soy protein isolate and gluten with the addition of NaCl and observed that fibrous macrostructures were formed with high water absorption characteristics. Chiang et al. [108] used a combination of wheat gluten and soy protein isolate in four different ratios along with the addition of soybean oil, wheat starch, seasoning, and the use of mechanical elongation ultrathin filaments that were heavily compressed to create a striated pattern resembling that of a chicken. Palanisamy et al. [34] used soy protein concentrate along with four different percentages of iota carrageenan which showed promising improvement in the meat analogues texture formation with harder, more fibrous, and less juiciness. Saldanha et al. [109] used faba bean protein concentrate in the designing of meat analogues and observed that meat analogues with good firmness, elasticity, and fibrousness. Aqueous fractionated soy protein fractions resulted in the making of fibrous structure meat analogues with a rise in water-holding capacity and viscoelastic characteristics [28]. Schreuders et al. [96] utilized a mixture of pea protein isolate and wheat gluten that emerged as the potential for preparing structured plant protein-based meat analogues.
The key steps of formulating and processing plant-based meat analogues using different processing techniques
Types of plant protein meat analogues
Emulsion type analogues
Finely chopped meat from various materials (such as hog, beef, mutton, etc.) is utilized in animal-based emulsion-type goods to create a steady blend, which links water and holds fat, offering the dish its distinctive texture when heated [16]. A variety of goods are created relying on the sorts of meat utilized, from premium all-meat sausages to economy-style sausages that have less superior meat cuts supplemented with more fat [88]. Though diverse sections of the animal are employed to make sausage, lean meat is often isolated first and combined with salt and water to extract the most protein. The remaining fat meat, spices, and binders are then combined with it to create the final product.
Soy protein, gluten, pea proteins, and potato proteins are among the plant proteins that can hold water and stabilize emulsions and gels. There is also the option of including proteins in a texturized state to generate a rougher texture in formulations of the emulsion type. However, non-protein binders or fillers like polysaccharides are frequently added to proteins (e.g., fibres and starches). It is widely recognized that the occurrence of plant proteins frequently results in a decrease in gel formation/elasticity in cooked emulsion goods, which is where the inclusion of those components comes from [110]. The latest product formulations like "mimic-würstel" and "mimic-mortadella" have recommended using tofu and fewer refined constituents, for instance, bean protein flour, chickpea flour, and wheat flour [111]. The dry matter composition of the goods is greater than that of their meat complements, among other things because of the utilization of these ingredient combinations.
Fat is an important ingredient because it enhances the juiciness, softness, and as whole mouthfeel of emulsion-type products. Moisture and fat binding must be stable in the highly hydrated gel protein matrix. For meat products, rind emulsions or fat pre-emulsions are employed to stabilize the fat, avoiding fat departure while cooking and agglomerate of the fat on the product's surface. Equivalent expectations are anticipated for plant-based contemporaries that employ plant oils and fats. For finely ground sausage applications such as frankfurters, the kind of fat (meaning less or large melting temperature) appears to be less significant, but fats with greater melting points are employed for making cooked coarse-cutting sausages or emulsion-type products with fat additions such as mortadella [36]. Such plant-based foods can have their fat stabilized by using native oleosomes or using plant proteins with high emulsification properties [112]. When heated, components high in protein that contain oil in their natural oleosome structure can also produce fat-comprising gels that may be suited for this kind of product [113].
To make the product mimic meat emulsion-type goods, colourants and spices are also included. Colors that are heat stable are employed, although they can also be naturalistic. For instance, to give plant-based bologna compositions (Smart Deli® Bologna by Lightlife) a traditional pink colour, paprika oleoresins and fermented rice flour were utilized. Depending on the kind of product the meat analogue imitates, a range of natural savoury spices and meaty scents are accessible [90]. Salt continues to be a crucial flavour enhancer. Nevertheless, it alters proteins' functionalities when it meets them [114]. There are significant obstacles in product formulation because of current dietary trends that strive to minimize salt and sodium content, particularly in sausage-type goods.
Burgers, patties, and nuggets
The goal of plant-based meat alternates that look like ground and bound meat from animals is to replicate its distinctive bite, chewiness, succulence, and firmness. Burgers, patties, and nuggets made from animal products mostly contain proteins and lipids with little amounts of seasoning, salt, and binders (for example, wheat crumbs, starches, and fibers). While binders help retain water and fat and enhance the texture and look of the product, salt alters the structure of proteins and toughens products (albeit in lesser quantities) [115, 116]. The recipes for comminuted plant-based products are very similar to those for analogous animal products. Many of the protein constituents are first converted into textured vegetable protein (TVP), a fibre structure that mimics ground meat, and then combined with the other nutrients to create the final composition.
Frequently, low moisture extrusion heating is used to texturize the protein. The soy, wheat, or pea protein-based TVPs, as well as their combinations, are the most often utilized TVPs in meat analogues. However, there are more and more protein sources that can be texturized and may be employed in the creation of novel plant-based burger-like products. In the final product formulation, hydrated TVP adds the desired juiciness and gives the product a meaty, chewy texture. The capacity of novel protein sources to maintain water in the storage period and free it during cooking and distortion are the main topics of research. Nonetheless, just like ground beef, TVP cannot be used alone to create a cohesive product, necessitating the usage of binders.
The major contenders in commercial products are egg protein and methylcellulose, although wheat gluten can also fill this character because it forms a network when wet and aids in binding TVP and other components. Texturizers that have a high water-holding capacity and can make the burger softer and juicier are used to further enhance the texture and mouthfeel of the items. Protein concentrates, protein isolates, and polysaccharides can all be employed to meet the latter ingredient needs. The product's fat, which can be a free, emulsified, liquid or solid plant-based fat, affects the feeling of juiciness as well. To attain the ideal balance, liquid fats (like coconut or palm oil) and solid fats (like sunflower and canola oil) are frequently combined (for example, see the Beyond Burger® and the Impossible TM Burger). Ideal burger fats should be liquid when heated and solid at room temperature. As a result, the food has a satisfying mouthfeel like that of related meat products.
Additionally, "bleeding" vegetarian burgers use beetroot juice to impart a recognizable meat hue while also attempting to impart a sense of juiciness. By creating new color-changing substances, flavourings, and fragrance precursors, research and development on plant-based burgers are also concentrated on obtaining even higher juiciness and enhancing the look and flavour of these goods.
Chicken-like and steak-like products
The imitation of whole-cut meats like chicken, pork, and beef steak, which are distinguished by the occurrence of long fibres or layered structures, is the goal of another category of meat analogue goods. Extrusion is used to create plant-based products that imitate this fibrous or layered structure. To obtain the desired final structure, colour, softness, aroma, and taste change, the items are treated more by freezing, curing, marinating, and cooking. Shear cell technology, which is currently being developed, has the prospective to produce big fragments of fibrous plant-based goods, whereas extrusion can currently only be used to produce small portions of similar products [117]. These products have the benefit that the end product's desired structure itself is present, so reconstitution is not necessary as it is with burger-type items. Due to the ability to exclude binders and other texturizing agents, this can drastically lessen the constituent catalogue. This implies, however, that the structuring stage is crucial to the development of both a fibrous and a juicy product.
Concentrates and other fewer refined formulas of soy protein, in addition to isolated soy protein, are employed in extrusion applications [25]. In several instances, a multi-phase blend is created with the aid of an isolate by adding extra ingredients like wheat gluten or carbohydrate fibres [88]. The alignment of those stages is then the basis for the mechanism of fibre production [117]. Finally, the structure solidifies often through cooling. The equipment utilised determines how the items are shaped. Due to the structural technology used, whole-cut-type meat analogues do not require binders in contrast to the previous meat analogue categories. Only a small amount of fat is introduced during the structuring process, but the texturized goods might afterwards be enhanced with fat (through marination). The industry prefers liquid oils for these kinds of products (like the vegan No Chicken chunks by The Vegetarian Butcher). Nonetheless, the potential for upgrading still exists, particularly when the goods are meant to resemble raw steak-like pieces where attractive marbling effects. For this reason, technologies to texturize vegetable fat are presently being investigated [117].
Contingent on whether the result simulates raw or cooked meat, colouring agents and flavours (comprising salt) can either be incorporated in the structuring process or administered as a marinade later. Most applications for flavour addition rely on marination since flavour components are harmed by the conditions utilized in an extruder. According to a patent by Giezen et al. [118], the wet extrudate product needs to be frozen first and then thawed before diffusion for the marination process by infusion to be successful. This indicates that after the extrusion process, cooling and freezing processes may be advantageous.
Some other representative examples
The addition of ginger, papain, and their mixture to camel meat burger patties during formulation led to a considerable rise in the collagen solubility and sensory scores of juiciness, tenderness, overall acceptability, and a significant reduction of the shear force values. Moreover, ginger extract and papain resulted in an improvement in the lipid stability of treated burger patties. Therefore, the addition of ginger extract and papain powder to the meat during the formulation of camel burger patties can improve their physicochemical characteristics and sensory properties during storage. Moreover, they can be applied on the industrial scale and household level as an easy method to improve camel burger patties' quality and prevent lipid oxidation during storage [119].
Camel meat burger patties were processed with the addition of ginger extract (7%), papain (0.01%), and a mixture of ginger extract (5%) and papain (0.005%). Lorenzo et al. [120] found that the wild Mediterranean fruits evaluated displayed intense antioxidant activity against protein oxidation and could play a key role as functional ingredients in burger patties by improving their oxidative stability and quality. The addition of Rubus ulmifolius would affect the color displayed by burger patties whereas the addition of Crataegus monogyna would supply some negative texture properties to these products. Some other fruits such as Rosa canina improve the oxidative stability, color, and texture of cooked burger patties with no apparent drawbacks.
Naveena et al. [121] indicated that both oil-soluble and water-dispersible carnosic acid (CA) extracted from dried rosemary leaves exhibited similar effects in inhibiting lipid oxidation in ground raw and cooked buffalo meat patties and chicken patties [122]. CA higher dosage (130 ppm) was highly effective in controlling lipid oxidation and metmyoglobin oxidation, thereby stabilizing ground buffalo meat and chicken lipids and raw buffalo meat color. However, the higher dosage of standard oleoresin (OxiKan-S10) exhibited a slightly “Spicy” flavor which shows the significance of refining antioxidants in meat applications.
Naveena et al. [121] determined the influence of sugar beet fiber (SBF) concentration on the rheological characteristics of meat emulsions and showed that SBF concentration caused an increase in apparent viscosity and meat emulsions behaved as weak gel-like macromolecular dispersions. Furthermore, based on his results, meat processors will be able to estimate the product structure and/or texture profile before a large scale of production is made [121].
Bahmanyar et al. [123] highlighted the properties of new meat products containing pseudo-cereals as high-quality plant protein [123]. The replacement of soy protein and bread crumb with quinoa and buckwheat flour in burgers was found to be effective on beef burgers characteristics. In this respect, the reformulated burgers can be used as replacers of soy protein and breadcrumbs in the beef burger formulations.
However, it is important to consider that consumer preferences in this study relied on a blind test of the burger samples. Future studies should provide consumers with information about the composition and nutritional benefits of the proposed samples so that information is also considered when preferring one burger sample over the other. As health risks associated with eating red meat and processed meat products are estimated to upsurge in the next ages, product reformulation using the proposed ingredients should be considered by meat processors to maintain or increase sales in a more demanding scenario [124].
Barros et al. [125] reformulated beef burgers to make them healthier through the total replacement of pork backfat with algal (Al) and/or wheat germ (WG) oils emulsions. The addition of oil emulsions increased the protein and decreased the proportions of lipids in the burgers between 26 and 38%.
Functional properties of plant proteins
The behavior of plant proteins involved in the designing of meat analogues is highly related to their functional properties [126, 127]. Contingent on the characteristics of plant proteins in the designing of meat analogues, these functional features can generally be distributed into three groups: (1) hydration characteristics; (2) properties related to interactions between protein molecules; (3) and the interface properties of proteins [126]. Functional characteristics of plant proteins, primarily contingent on amino acid composition and molecular structure, directly influence texture, appearance, and stability of meat analogues, and ultimately determine preparation, processing and storage of food or ingredients, as well [128]. Studying the functionality of food proteins is essential so that their role may be fully understood, and they may be used effectively in the designing of meat analogues. Table 5 gives a list of the essential qualities that plant proteins naturally possess and their functional characteristics.
Bulk density of plant proteins
In industrialized meat analog processing, plant protein materials generally exist in the form of powder. The bulk density is a critical parameter for powdered materials as it affects package size and method, the fluidity from one container to another through pipes, and solubility in the formulating process [129]. The bulk density is mainly linked to the surface properties of the protein materials, composition, and consolidating stresses [90, 130]. The bulk density of most plant protein materials in different forms follows in the range of 0.1 to 0.6 g cm−3 (Table 5). According to the report by Özdemir et al. [131] freeze-dried protein powder (0.13 cm−3) from industrial sesame processing waste had lower bulk density than the spray-dried one (0.32 cm−3).
Alonso-Miravalles et al. [130] found that the protein-rich flours had lower initial bulk density values (0.24–0.47 g cm−3) than the regular flours (0.34–0.63 g cm−3) from pseudocereals (amaranth, buckwheat, quinoa) and cereals (rice and maize). The plant protein materials display higher bulk density at higher consolidating stresses. Therefore, soy press cakes have a much higher bulk density (1.10 g cm−3) than flours and protein powders [132]. The powders tend to compress under self-weight during storage, which may result in increased bulk density and alter their handling properties (such as fluidity). Whereas plant protein materials with low bulk density may pose a high risk of oxidation due to the presence of oxygen in intergranular spaces [130].
Solubility of plant proteins
Solubility is the first functional property usually determined during the development and testing of new protein ingredients, which is because it is a pre-requisite for other functionalities including the emulsification property, foaming property, and gel-forming ability, etc. [135, 152, 153]. Lee et al. [129] determined the solubility of red lentil protein isolates and found that their solubility patterns were similar. According to the available literature [129, 134, 135, 154]. The solubility of all plant proteins exhibits a typical U-shaped curve with the lowest value observed at the isoelectric point. The isoelectric point of proteins from various plant seeds, oil processing by-products, flour, and tree leaf is reported to be 4.0 to 5.0 (Table 6), which is slightly lower than that of myofibrillar proteins from muscle meat (5.0–5.2) [155]. The solubility of proteins is affected by environmental aspects (ionic strength, type of solvent, pH, temperature, etc.) and processing conditions [134, 137]. Among the environmental factors, the pH that determines zeta potential affects the solubility the most pronouncedly [154]. The research recommended that plant proteins could be appropriate for alkaline formulation foods since the solubility is significantly higher at alkaline pH than at acidic pH [134, 137]. Carbohydrates like polyphenols would form nanoparticles with proteins reducing protein solubility [154].
Water retention capacity of plant proteins
Water retention/holding capacity represents the ability to hold water without protein dissolving, which influences food texture, shelf-life, and quality characteristics of the meat analogues [126]. Generally, higher water retention capacity is desirable as tender and juicy meat analogues can be designed; however, excessively high-water retention capacity may dehydrate other ingredients in food formulations resulting in deterioration of overall quality [139]. The water retention capacity of plant proteins from distinct bioresources varies greatly, from 1.0 to 7.0 g g−1 [129, 133, 139, 140]. Wang et al. [133] reported that proteins recovered from avocado oil processing by-product showed a much higher water retention capacity (6.60 g g−1) than that of soy protein (4.69 g g−1). The water retention capacity of plant proteins is influenced by composition (especially polar hydrophilic groups) and conformation of the protein molecules, environmental factors, the presence of other components, and processing and storage conditions [129, 133, 139, 140]. Water-loving components (e.g., dietary fiber) from plant material generally contribute to a higher water retention capacity [154]. Protein is extracted from plant materials and then used for meat analog processing. Mohan and Mellem [140] indicated that the natural conformation of proteins from hyacinth bean seed was disrupted during the extraction and precipitation steps thereby reducing the protein interaction with the aqueous environment and leading to a low water retention capacity [140].
Fat retention capacity of plant proteins
Fat retention capacity is a measurement of the ability of non-polar side chains of proteins to bind fat. It plays a potent character in improving the flavor of meat analogues and reducing the rate of fat oxidization [126]. The fat retention capacity of plant proteins showed significant differences among samples of different species and origins [129]. Fat retention capacity of proteins from soybean seed, walnut, tree peony, avocado oil processing by-product, Amygdalus pedunculata pall seed, red lentils, and hyacinth bean seed is determined to be 2.43, 2.81, 6.93, 5.53, 3.54, 4.57, 5.8–7.3, 2.37–2.99 g g−1, respectively [129, 133, 139, 140]. Li et al. [135] asserted that bell pepper protein isolates with a fat retention capacity of 4.57 g g−1 could be exploited in the food industry, such as in meat substitutes and extenders. Fat retention capacity is affected by hydrophobicity, charge, surface area, and size of the macromolecule [129]. Therefore, the higher fat retention capacity values in comparison with the water retention ability of plant proteins, reflect the higher ratio of non-polar (hydrophobic) to polar (hydrophilic) amino acids [140].
Emulsifying property of plant proteins
The emulsion property of proteins is commonly measured by the emulsification capability index (EAI) and emulsification stability index (ESI). EAI evaluates the capacity of a protein to adsorb at the water–oil interface and reduce interfacial tension, whereas ESI is a measure of the ability of an emulsion to maintain its structure stable over a defined period [136]. These two indexes are critical parameters that determine the choice of plant protein for use in meat analogues, as they affect the qualities like texture (creamy versus greasy), color, appearance, stability, mouthfeel, etc. [140]. The functionality of protein in stabilizing emulsion is due to its amphiphilic molecular structure. Specifically, after mechanical mixing (homogenization, microfluidization, etc.) protein acts as emulsifiers using forming a film or skin around oil droplets that are dispersed in an aqueous medium to prevent structural change and phase separation of the emulsion system [136]. Compared with other functionalities of plant protein, the emulsion properties of different raw materials are significantly different. For example, the EAI of quinoa seed protein is 1.24–3.38 [69]. The EAI of hyacinth bean seed reaches 88.89–100, about 50 times that of quinoa seed protein [140]. The ESI of plant proteins from different sources ranged from 2.31 min to 46.34 min [69, 127, 129, 133, 139, 140]. EAI and ESI are dependent on the properties of proteins, environmental factors, and conditions of the emulsification [140].
Foaming property of plant proteins
Foaming property is evaluated by the foaming capability index (FCI) and foaming stability index (FSI). FCI means the capacity of a protein to make a foam under certain conditions (such as temperature, concentration, pH, whipping, etc.) due to air incorporation, whilst FSI is how effective a protein is in maintaining a foam during a fixed time [135]. Soluble proteins or aggregates migrate to the interface of the air–water, which reduces surface tension and keeps air bubbles in suspension, thus slowing the rate of coalescence. Recently, Zhu et al. [156] found that wet-separated pea protein had better foaming properties than that of wet-separated one, and the resulting dough of meat analogues was more solid-like with higher hardness. FCI of proteins from bell pepper seed, quinoa seed mung bean, hyacinth bean seed was reported to be 152.67–354.33, 58.37–78.62, 62.50, and 30.33–123.33, respectively, and the corresponding FSI was 113.33 to 119.00, 54.54–83.55 95.20%, and 27.32–84.44%, respectively [135, 136, 140]. The foam foaming property generally depends on protein solubility, as proteins with high solubility can diffuse easily and rapidly into the air–water interface for air bubble encapsulation, leading to improvements in FCI and FSI [136]. At present, the effect of the foaming property of plant protein on the quality of meat analogues is still lacking.
Gel forming ability of plant proteins
Gel-forming ability is the aggregation of unfolded proteins to form a 3D microstructure network through intermolecular interactions [143]. It is usually measured by the least gelation concentration (LGC) and gel strength (GS). Gel property is the foremost indicator for evaluating the usage of plant proteins in meat analogues. The gel-forming ability of plant proteins from diverse sources is significantly different. For example, when the concentration of mung bean protein is above 13%, it can form a gel [157]. The LGC of hyacinth bean seed and soy protein isolate is 16% and 15%, respectively [140, 143]. However, the LGC of rice protein isolate must reach more than 35% to make a gel [143]. The gel strength of plant proteins is significantly lesser as compared to proteins of meat flesh [155]. The nature and concentration of protein, environmental factors, and processing conditions are important influencing factors in the creation of gel [143]. Liu et al. [136] found that the neutral and alkaline environments in mung bean proteins were favoured to denature and unfold the proteins and expose the more embedded functional groups under heating, which improved the molecular interactions and gel texture.
Film forming property of plant proteins
Water vapour permeability (WVP) and tensile strength (TS) are the two critical parameters of film. The WVP of the film made from quinoa seeds, sesame seeds, and mung bean seeds were reported to be 1.98–4.76, 10.87–13.57, and 10.76 10−7g Pa−1 h−1 m−1, respectively and their TS were 1.88–4.28, 8.29, and 3.33 MPa, respectively [144,145,146]. The film-forming property can be influenced by the properties of proteins used for preparing the film such as solubility, the hydrophobic/hydrophilic nature, purity, free volume, molecular mobility, and flexibility [144,145,146]. Yang et al. [158] used proteins from distiller-dried grains to prepare film incorporating green tea extracts and reported that the film can be utilized as an anti-oxidative packaging material for pork meat. Plant protein film has the potential to be used for packaging meat analogues. However, there are few relevant reports at present.
Binding property of plant proteins
In meat analogues processing, adding flavor (such as vanillin) and nutrients (such as flavonoids) is easy to achieve. Protein contains a variety of functional groups, which can interact with flavonoids, vanillin, quercetin, rutin, and other compounds through covalent (Schiff bases) and non-covalent (hydrogen bond, hydrophobic interaction, electrostatic force, etc.). Therefore, on one side, proteins can bond flavonoids and anthocyanins reversibly and irreversibly to form complexes and improve their stability. Jia et al. [147] stated that 7S/11S soybean protein can bind quercetin and rutin. The binding constant was 0.03–97.43 105 L M−1, and the binding site was 0.77–1.65. Soybean protein isolate was reported to be able to bind to flavonoids, with a binding constant of 0.23–143.88 105 L M−1 and a binding site of 0.98–1.75 [147]. On the other hand, proteins can interact with vanillin, aldehydes, and ketones to cause the loss of flavor intensity or so-called flavor fade. Temthawee et al. [148] found that the binding of vanillin to coconut protein was enthalpy driven, the binding constant was 40.1–122.2 105 L M−1, and the binding site was 0.81–1.48 [148]. The interactions between the compounds and proteins can be influenced by several factors relevant to the functional groups of these compounds and the changes in the protein conformation [147, 148].
Extrusion ability of plant proteins
Extrusion is the most widely used technology to process plant proteins to meat analogues with rich fibrous structures and good springiness like real animal meat. Specific mechanical energy (SME) and fibrous degree (FD) are the most important indicators of extruded meat analogues. SME refers to the mechanical energy absorbed per unit mass of extrudates, which translates into the extent of molecular collapse or disintegration of materials during extrusion. The FD was computed by dividing the crosswise shear force lengthways, which can be used for characterizing the anisotropic structure in the extrudate. Soy protein concentrate, pea protein isolate, and peanut protein powder have been used for extruding into meat analogues [149, 150, 159]. Their SMEs were 1029.03, 985.07660.56–1135.67 kJ, respectively, while TD is 1.03, 1.30, and 1.33, respectively. SME is majorly connected with the contents of moisture and fat, and energy input intensity [151, 160]. Fatty acids, especially those with low unsaturation degrees, have a lubrication effect, which reduces die pressure and contributes to the smooth flow of protein melt in the extruder barrel, consequently reducing the mechanical energy consumption during extrusion processing. TD is related to the protein nature, functional additive, and operation conditions. Dou et al. [149] reported that adding Gums promoted the fibre formation.
Influence of processing on functionalities of proteins
The functional qualities of plant protein depend on processing procedures intrinsic to the chosen extraction processes, modification, heat treatment, etc. in addition to elements inherent to the protein and environmental conditions [161]. These treatments will cause desired and unwanted changes in the functional characteristics of proteins (Table 6). In this way, it is very necessary to explain the changes in protein functional properties during processing operations and the corresponding results from the perspective of chemistry and physics.
Effect of physical operations on proteins
Effect of high-pressure homogenization, micro-fluidization, and high hydrostatic pressure treatments
In recent years, high-pressure processing has received attention from both industry and academia and has smeared extensively to amend the functional characteristics of plant proteins. During the high-pressure homogenization process, a continuous flowing fluid or suspension is pushed through a narrow gap that is usually controlled by a valve, which leads to high turbulence and shear stress [85]. Micro-streams with high velocity are generated in the micro-fluidization process, as fluid is accelerated into a Y-type interaction chamber by a high-pressure pump, resulting in high shear and impact forces [152]. In high-pressure homogenization, the fluid circulates in the equipment for a period, whereas the fluid passes through the micro-fluidization device in a fleeting time. As for the high hydrostatic pressure treatment, protein isolate or concentrate is placed in a closed ultra-high-pressure container statically, and water is used as the medium to apply a pressure of 200 ~ 600 MPa usually, which is higher than that (typically in a range of 50–200 MPa) in the micro-fluidization and high hydrostatic pressure treatment [165].
Those pressure effects can induce significant modifications of the functional characteristics of plant proteins (Table 6). Regardless of the method and protein source, moderate pressure (50 ~ 200 MPa) treatment can significantly increase the solubility, emulsification property, foaming property, and gel-forming ability. The improvement of solubility can be attributed to the fact that moderate pressure treatment causes the proper dissociation of the quaternary structure, the diminution of protein particle size, and the swelling of the molecule, leading to an increase in solvent-protein interaction [166]. At the same time, moderate pressure treatment unfolds the protein conformational structure, which led to the disclosure of internal hydrophobic groups and the increase of molecular flexibility, thereby enhancing the intermolecular interactions and protein adsorption at the air–water and oil–water interfaces. Therefore, the foaming property, gel-forming ability, emulsification property, and film-forming property are improved. However, excessive pressure (> 300 MPa) treatment induces the creation of bigger protein aggregates, causing declined solubility and other functional characteristics [162,163,164]. The effects of shear stress and impact force during the pressure treatment have often been ignored, which would have effects on the functional characteristics of proteins.
Effect of sonication processing
Sonication is a famous processing operation and has been successfully used either for increasing extraction yield or improving the functional characteristics of the plant proteins obtained from diverse sources (Table 6). The consequences of sonication on food proteins’ functional characteristics are attributed to cavitation. Cavitation causes massive shear, turbulence, and temperature rise when the neighbouring bubble collapses. The key parameters correlated with sonication are ultrasound frequency, operating time, power, or intensity. Researchers have pointed out that concentration of protein, pH, and ionic strength are also important parameters that need to be considered [133, 143].
Protein solubility of numerous sources including pea protein isolates, and grass pea protein isolate gradually increases when the sonication power increases [146, 167]. The incline in the protein solubility is owing to the sonication cavitation, which lessens the particle size of the protein molecule and/or aggregates by disrupting intermolecular interactions (hydrogen and hydrophobic interactions particularly), making proteins a larger surface area to contact with water [167]. Mozafarpour et al. [146] assessed that the solubility of grass pea protein isolates amplified and afterwards declined when the sonication duration boosted from 5 to 20 min. Furthermore, the solubility of proteins from bell pepper seed decreased after sonication at 350 W for 140 min [154]. Sonication treatment resulted in the disclosure of hydrophobic groups of amino acid remains, which might be a key factor in the decline of solubility.
The changes of other functional properties including ORC, WRC, foaming property, gel-forming ability, emulsification property, film-forming property, and extrudability by sonication are associated with the solubility. ORC, which indicates fat-binding performance, is highly correlated with the hydrophobic properties of a protein. Therefore, after sonication plant proteins generally exhibit an increased OHC, which is mainly owing to the surface disclosure of some hydrophobic regions of proteins [133, 143]. Furthermore, the incline in solubility contributes to the increase of the ORC. WRC is an indicator of the performance of water binding and /or entrapping, which is correlated with the solubility and hydrophilic properties of a protein. The alteration of WRC by sonication is determined by sonication conditions and protein source [133, 143]. The exposure of hydrophobic groups induced by sonication facilitates the diffusion of protein molecules toward air–water or oil–water interfaces and their adsorption on them. Consequently, the foaming property and emulsification properties are remarkably improved on the condition that the structural changes have been balanced in terms of hydrophilicity and hydrophobicity after sonication [143, 153]. Although the hydrophobicity increases, the foaming property, and emulsification properties may decrease due to the decline in the solubility under the excessive sonication [133, 143]. Under moderate sonication conditions, gel-forming ability film-forming property, and extrudability increase, as indicated in the increase of TS while the decrease of WVP, a decrease of LGC, and an increase of TD, correspondingly [143, 144, 168]. The reason might be assigned to the partial unfolding of their three-dimensional molecular structures, resulting in the exposing of hydrophobic and/or sulfhydryl groups, thereby promoting the formation of more interconnected gel networks due to the presence of more junction zone per particle [143, 168].
Effect of water bath incubation, autoclaving, ohmic heating, microwave heating, and extrusion cooking
Heat treatment is a traditional processing method, including water bath incubation, autoclaving, ohmic heating, microwave heating, extrusion cooking, etc. These heating methods have distinct characteristics. For example, water bath incubation is easy to apply in industrial production. Autoclaving can make the material temperature reach over 100 ℃. Ohmic and microwave heating can quickly generate heat by utilizing the friction movement of polar molecules and the conductivity of ions, respectively, thus shortening the heating time. Extrusion cooking combines the functions of mixing, sterilization, heating, drying, and forming. Heat treatment affects the functional characteristics of plant proteins.
Generally, the solubility of protein decreased after thermal treatment, which is mainly due to the creation of insoluble aggregates [139, 165]. However, Hu et al. [166] reported that extrusion increased the solubility of Baijiu vinasse proteins and suggested that the changes in solubility during extrusion are primarily due to an interplay of shearing, temperature, and pressure, which led to the formation of the small particle size, porous structure, and air voids of proteins. Water bath incubation, ohmic heating, and extrusion cooking affect the foaming property and emulsification properties of proteins, which rely on the operation conditions. The changes in the foaming property and emulsification properties can be explained by the changes in solubility and conformational structure [139, 166]. After water bath incubation (90 °C), the gel-forming ability of cowpea protein isolates decreased. It could be due to the formation of aggregates that had a lower ability to realign and form the protein network [165]. Guo et al. [169] examined that the binding capacities of soy protein isolate for HxAc and HpAc decreased as the temperature increased in the protein aqueous solution. It was related to the formation of an additional hydrophobic surface because of the thermal denaturation (unfolding) of protein, which declined the affinity of primary binding sites. Whereas the binding capacities of soy protein isolate for LiFo, LiAc, linalool, and geraniol increased, the reason was that heat treatment increased the number of lower affinity secondary binding sites on the hydrophobic surface of soy protein isolate. TD showed a tendency to significantly decrease after autoclaving [170]. The result was thought to be related to the movement and redistribution of moisture caused by the vacuum-heat treatment process.
Effect of atmospheric cold plasma, ultraviolet radiation
In recent years, non-thermal technology, a potential alternative to traditional thermal processing for microbial inactivation to extend the shelf life, including atmospheric cold plasma and ultraviolet irradiation, etc., were pertained to improve the functional characteristics of plant proteins regarding solubility, gel-forming ability, film-forming properties, and foaming property [145, 172, 173, 186].
The active species produced by atmospheric cold plasma including reactive oxygen species (ROS) and reactive nitrogen species (RNS) can break covalent bonds and initiate some chemical reactions. Zhang et al. [187] studied that the pea protein concentrate could form a gel at a lower concentration than native pea protein concentrates and possessed better mechanical strength. Their results revealed that oxidization by atmospheric cold plasma treatment contributed to the unfolding of the rigid structure of pea protein, the exposure of hydrophobic groups and free sulfhydryl groups, and the enhancement of the gel-forming ability. Fathi et al. [145] employed electromagnetic radiation induced by ultraviolet (UV) light to enhance film film-forming characteristics of sesame protein isolate and found that WVP was decreased, and tensile strength was improved after UV exposure [145]. UV radiation uptake by double linkages and aromatic rings in plant proteins instigates the creation of free radicals in amino acids, thereby resulting in the creation of intermolecular covalent linkages [145]. Therefore, the film-forming characteristics of sesame protein isolate were improved.
Effect of ball milling operation
Planting raw materials often needs to be reduced in size before processing, to improve the extraction rate and reaction rate. Plant protein is broken or fractioned in various ways, among which, ball milling has been reported as an efficient and eco-friendly processing method [157]. Besides size reduction, a mechanochemical effect is produced by this process via the collision, friction, and shear between the milling balls and the container wall after multiple high-energy collisions, which cause the partial or complete denaturation of plant proteins, thereby improving the functional characteristics, comprising foaming property, emulsification property, water retention capacity and gel-forming ability [157, 188]. Owing to the mechanochemical effect, the protein molecule rearrangements via the alterations in electronic arrangement and crystal structure. As a result, the secondary structure of proteins became looser and more disorderly, and free sulfhydryl groups and surface hydrophobicity increased. It should be noted that if the ball milling time is too long, the particle size of the material will not decrease or even increase under the action of van der Waals force and electrostatic force. On the other hand, protein will be over-denatured, resulting in a decline in functional properties [157].
Effect of freeze-drying and spray-drying
Reducing the water content (more accurately, the water activity) of plant protein through drying can protract the shelf life of products, and lessen food volume and weight, save packaging, transportation, and storage costs. Freeze drying is the most common method used to dry protein isolates or concentrate in the laboratory. It is frequently thought to be less damaging to proteins than spray drying because the sample is dried by sublimation at low temperatures. However, spray drying is practical for industrial-scale plant protein dehydration. In spray drying, the protein solution can be dried into powder by warm air within a few seconds after being atomized into droplets.
Regarding functional properties, Acosta-Domínguez et al. [174] reported that soy protein isolates subjected to freeze drying presented lower bulk density, higher oil, and water retention capability, and higher emulsifying and gelling capacity than native soy protein isolate. Burger et al. [175] examined the impacts of temperature and pH on the functional characteristics of pea protein isolate and reported that protein solubility inclined and further declined as the inlet temperature increased from 165 to 195 °C, while the solubility constantly increased as the pH inclined from 5.0 to 9.0. A comparative study on the functional characteristics of plant protein by these two drying methods has also been reported [175]. Peanut protein concentrates subjected to spraying drying had higher emulsifying capacities than the ones by freeze drying, but lower solubility, and water/oil retention capacity [189]. Likewise, results are also reported for protein isolate from rice dreg protein [190, 191]. The impacts of the drying method on the functional characteristics are highly related to the conformational structure change after drying.
Effect of chemical operations on proteins
Effect of pH-shifting
pH-shifting is a process universally employed to purify plant proteins; it is a simple procedure that resolves proteins in a pH far away from the isoelectric point (> 10 or < 2), and then precipitates the proteins at the isoelectric point. The pH-shifting has also been applied to chemically modify proteins. In an adverse acidic or alkaline setting, the proteins unfold the conformational structure from globular to one that is known as the “melted globular” or flexible structure, via the weakening side-chain protein interactions under the acidic or alkaline conditions, to affect its functional properties. Previous studies have reported that the solubility, emulsification capability, and gel-forming ability of plant protein were improved by pH-shifting [176, 177, 192].
Liu et al. [176] examined the impacts of low-pH-shifting treatment (pH 7 → 2 → 7) on the solubility of soybean protein isolate and found that pH cycling treatment enhanced solubility. They speculated that exposure of hydrophilic groups and degradation of protein particles were the two reasons for the enhanced solubility. Soybean protein molecules were dissolved at pH 2. When the pH was readjusted to 7.0, the soybean protein molecules maintained the conformation to some extent, resulting in a high solubility in a neutral environment [176]. However, the opposite result was reported in the wheat gluten protein by Xiong et al. [177]. The protein treated has a distinct structure (hydrophobically accumulated) when resumed to neutral circumstances, according to their hypothesis, which contends that the lower solubility was caused by hydrophobic accumulation under severely acidic circumstances. Whether the solubility is reduced or increased, the emulsifying capability of plant proteins from different sources reported in the literature has increased or decreased [176, 177]. Correlation assessment uncovered that conformation examines the emulsifying characteristics of SPI. the pH-shifting treatment causes greater β-sheet and sulfhydryl contents, and greatly disclosed hydrophobic groups, improving the amphiphilicity of the proteins.
Effect of glycation, phosphorylation, acylation, deamidation, cationization
The chemical modifications including glycation, phosphorylation, acylation, deamidation, and cationization, etc. have been applied to improve the limited application of plant proteins (like rice protein, peanut protein, coconut protein, walnut protein, etc.) in the food industry owing to their low solubility at neutral pH and this feature is highly associated with functional properties. Glycation is a popular modification approach that involves a condensation reaction between the primary amine of proteins and the carbonyl groups of reducing sugar side chains via Amadori rearrangement of the Maillard reaction, enabling the protein to be covalently connected with hydrophilic groups [150]. Phosphorylation modification of proteins refers to the creation of novel chemical linkages (O–Pi) between inorganic phosphoric acid and the oxygen atoms on the residues of specific amino acids (serine, threonine, tyrosine, etc.) in proteins, or the formation of new chemical bonds (N-Pi) with the nitrogen atoms on the residues of specific amino acids (lysine, histidine, arginine, etc.) [178]. Acylation is a nucleophilic substitution reaction between acylating agents (e.g., succinic/acetic anhydride) with protein amino acid residues (chiefly lysine) [179]. Chemical deamidation refers to the conversion of glutamine and aspartic acid in protein into glutamic acid and aspartic acid through limited hydrolysis using hydrochloric acid usually [180]. During cationization in alkaline aqueous media, the quaternary ammonium groups are introduced into the nucleophilic sites of the protein [181]. The essence of the above modifications is to enhance the functional characteristics of plant proteins by changing the structure or conformation of proteins, electric charges, hydrophilic and hydrophobic properties, etc. [180, 181].
Solubility of various plant proteins including rice protein, pea protein isolate, coconut protein, and soybean protein isolate is significantly improved by glycation, acylation, deamidation, and cationization [178,179,180,181]. The increased solubility by that chemical modification can be attributed to three aspects: (1) the increase of net charges which unfold and dissociate the quaternary structures and increase repulsion between protein chains (acylation, deamidation, and cationization); (2) the steric effect which inhibits protein re-aggregation (glycation); (3) the enhancement on the affinity of the conjugate or proteins to water molecules (acylation, deamidation, glycation, and cationization). The emulsification capability of plant proteins is improved by glycation, phosphorylation, acylation, and deamidation, and forming capability by glycation, phosphorylation, deamidation [150, 178, 180]. The increased emulsification capability and forming capability can be explained by the enhanced solubility, and the formation of balanced amphiphilic molecule adsorbing at the oil–water and air–water interfaces. According to the reports by Sánchez-Reséndiz et al. [178] and Shen and Li [179] WRC and ORC of soybean protein isolate, and pea protein isolate were improved by phosphorylation and acylation. The increase in WRC is related to the increased solubility, and the higher ORC is due to the exposure of more hydrophobic amino acid residues of the protein. LGC of pea protein isolate was remarkably decreased by acylation, which was due to the disclosing of the protein via conjugation-enhanced protein hydrophobic interaction in the creation of a more stable gel network, thereby lessening the number of proteins needed for gel making [179].
Effect of biological operations on proteins
Effect of enzymatic reaction
The enzymatic reaction is carried out either via removing the corresponding groups (e.g., deamidation), partial hydrolysis (e.g., protease), or covalent cross-linking (e.g., by transglutaminases). Sun et al. [182] used complex protease to partially hydrolyze glutelin protein recovered from walnut cake and found the modified walnut protein increased the solubility by ~ 1.33 times, the WRC by ~ 0.23 times, the emulsify capability by ~ 0.32 times, and the emulsion stability by ~ 0.75 times. The improvement of these functional properties could be attributed to the reduction of molecular size, the exposure of amino acid residues such as glutamic acid and aspartic acid, and the enhancement of the amphipathic property of the protein. A remarkable increase in TS and a decrease in WVP were observed after the treatment of composite films with microbial transglutaminase (MTGase), which was due to the polymerization of proteins [183]. According to the results of Pöri et al. [184] that the enzymatic modification of oat proteins by cross-linking and deamidation can improve fibrous structure formation of oat protein concentrate (OPC) during high-moisture extrusion processing due to the creation of a stronger protein network [184].
Effect of fermentation
Fermentation by microbial proteolytic enzymes is a traditional processing approach in the food industries. However, compared with more methods, fermentation is relatively less applied to enrich the functional characteristics of plant protein. Meinlschmidt et al. [185] investigated liquid-state fermentation on the functional characteristics of soy protein isolate. According to their results, fermentation increased protein solubility at pH 4.0 while decreasing the solubility at pH 7.0. The microorganism produced a large amount of acid, which led to the irreversible coagulation of proteins and thereby decreased protein solubility at pH 7.0. As a result, the capacity of soy protein to form an emulsion was negatively affected. Although protein solubility decreased, WRC, ORC, and foaming activity significantly increased compared to non-fermented SPI. The reason was because of the partial hydrolysis of soy proteins, causing the formation of more flexible molecules.
Conclusions and future perspectives/trends
The subject of plant-based meat analogues has been the primary topic of conversation in the food area for quite some time because of expanded concern connected with the well-being influences and supportable advancement of meat choices. People may be more willing to substitute their meat consumption by creating meat analogues, which copy meat with both its nutritional content and its physical sensations. As a result, understanding the study findings on the creation, enhancement, requirement, sustainability, and usefulness of meat analogues is critical in developing a plan for future research in this sector. As a result, this review provides a thorough discussion of the importance of developing meat analogues, the health risks associated with producing meat products, the sources of plant proteins that can be used to develop meat analogues, the functionality of the ingredients used to develop these products, and consumer attitudes towards plant-based meat alternatives. The purpose is to assess the present status of scientific research on PBMA and estimate future research opportunities. Product development is difficult due to the wide range of ingredient functionality requirements across the many forms of plant-based meat substitutes (sausages, burgers, and meatballs). In general, meat analogue applications do not benefit from the functional properties of readily available protein-rich ingredients, the majority of which are highly purified from plant material. The need to use additives to improve product textures is critical. As a result, prospective research must be done to update the functioning of these novel food products and boost public knowledge of plant-based meat substitutes to increase consumer acceptance. Other fractionation techniques, which prioritize functionality over purity, can produce novel functionality. Additionally, novel proteins can provide novel ingredients for meat analog applications.
Data availability
There is no data available for this article.
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Open Access funding enabled and organized by Projekt DEAL. The open access publishing fee is covered under the agreement between the DEAL Consortium and Springer and Springer Nature upon acceptance due to Shahida Anusha Siddiqui being affiliated with the Technical University of Munich.
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Shahida Anusha Siddiqui—Conceptualization, Methodology, Writing—Original Draft, Writing—Review and Editing, Validation, Formal Analysis, Investigation, Software, Data Curation, Visualization, Resources, Project administration, Funding Acquisition, Supervision. Ibrahim Khalifa—Writing—Original Draft, Resources, Visualization. Tao Yin—Writing—Original Draft, Visualization. Mohamed K. Morsy—Writing—Original Draft, Visualization. Ramy M. Khoder—Writing—Original Draft, Visualization. Molla Salauddin—Writing—Original Draft, Visualization. Wasiya Farzana—Writing—Original Draft, Visualization. Sonu Sharma—Writing—Review and Editing, Visualization, Validation. Nauman Khalid—Conceptualization, Review and Editing, Supervision.
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Siddiqui, S.A., Khalifa, I., Yin, T. et al. Valorization of plant proteins for meat analogues design—a comprehensive review. Eur Food Res Technol (2024). https://doi.org/10.1007/s00217-024-04565-1
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DOI: https://doi.org/10.1007/s00217-024-04565-1