Abstract
The synthesis of bioactive peptides demonstrates strong antioxidant, anti-proliferative, anti-hypertensive, and anti-diabetic attributes. This presents a promising path for developing cost-effective pharmaceuticals that have fewer side effects as they are derived from foods. Production of bioactive peptides through enzymatic hydrolysis exhibits greater potential compared to alternative chemical-assisted hydrolysis. The purification of bioactive peptides involves size fractionation techniques such as ultrafiltration and gel filtration. Further separation using reversed-phase high-performance liquid chromatography (RP-HPLC) techniques aids in the production of peptides with different hydrophobicity which may have specific bioactivities. Sequencing of peptides is commonly completed through Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry (MALDI-TOF MS), electrospray ionization (ESI), and Liquid chromatography-tandem mass spectrometry (LC–MS). Generally, smaller peptides with lower molecular weights exhibit higher bioactivity due to higher absorption within the gastrointestinal tract. While most investigations into bioactive peptides have been conducted in vitro only a few studies have confirmed these findings in vivo, particularly regarding the bioavailability and toxicity of fish protein peptides especially in individuals with non-communicable diseases (NCDs) such as cancer, cardiovascular, diabetes and chronic respiratory. Bioactivities of peptides derived from fish show cardioprotective, anti-hypertensive, anti-cancer, anti-diabetic, and anti-oxidative effects, suggesting their promising potential in the treatments and preventive care for NCD. Further research is strongly encouraged to explore these aspects comprehensively.
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1 Introduction
Non-communicable diseases (NCDs) including cancer, cardiovascular, diabetes, and chronic respiratory disease account for 74% of worldwide mortality [1]. A significant amount of non-communicable disease (NCD) deaths, 86% of individuals encounter premature death before reaching the age of 70. NCDs comprise a significant portion of death and disability in adults, and risk factors are introduced at a young age [2, 3]. Chronic diseases are characterized by prolonged disorders caused by a combination of hereditary, biological, environmental, and psychological variables [2, 4]. NCDs quickly spread worldwide and have reached epidemic proportions in many countries due to globalization, industrialization, increasing urbanization, and demographic and lifestyle changes [5].
The global pandemic of non-communicable diseases creates a significant threat to sustainable growth. Non-communicable diseases (NCDs) are also included within the scope of Sustainable Development Goal (SDG) 3.4. This goal sets a target to decrease premature mortality caused by NCDs by one-third by the end of 2030. Additionally, SDG 3.4 intends to promote psychological wellness and health using early detection and treatment strategies [6, 7]. In recent years, significant growth in epidemiological data has been directly linked to the prevalence of non-communicable diseases in people of all ages. A functional food comprises any food that, in addition to basic nutrition, offers a health benefit to one or more biological processes [8, 9].
Fish protein is an essential and significant dietary component, particularly in regions with developing and developed countries. The global population relying on fish production, processing, and trade for their livelihood is estimated to be about one billion individuals [10,11,12]. The fish processing operations yield over 60% of by-products classified as trash, including various components such as skin, head, fins, trims, frames, internal organs, and roes. Conversely, only 40% of the fish products derived from this sector are intended for consumption by humans directly [13,14,15,16]. The substantial quantities of discarded fish by-products generated by fishing activities pose significant environmental concerns related to pollution and disposal, impacting countries at various stages of development. The residual waste materials comprise a substantial quantity of protein-rich substances typically transformed into commodities of limited economic value, including animal feed, fishmeal, and fertilizers [17,18,19]. Numerous biotechnological methods have emerged for harnessing the protein-rich by-products generated from fish processing. These techniques aim to extract vital nutrients and bioactive compounds. This supports human health by offering protection against diseases supplying essential nutrients and addressing pollution and disposal challenges [20, 21].
To harness the nutritional potential of fish processing waste, low-value fishes and underutilized fish resources are viable strategies that involve their transformation into fish protein hydrolysates [22]. Fish protein hydrolysates are presently regarded as significantly rich in protein and an excellent source of bioactive peptides [23]. Protein hydrolysates typically consist of short peptide fragments comprising 2–20 amino acids [24, 25]. Proteolytic cleavage of proteins into various peptides and amino acids enhances the bioavailability of amino acids in hydrolysates, making them a highly accessible source of amino acids for a variety of human physiological processes [26]. Protein hydrolysates are bioavailable and functional food ingredients that are readily available and widely used in human and animal diets [27]. Food scientists have shown significant interest in fish protein hydrolysates for a variety of food and pharmaceutical sectors due to their excellent nutritional content, amino acid profile, and biomedical properties [22, 24]. Various studies have revealed that hydrolyzed proteins possess a wide range of biological characteristics, including antioxidant [28,29,30], antiproliferative [29] anti-inflammatory [30], antimicrobial [30] and anti‐hyperglycemic activities [31].
This article examines the various techniques employed in the production of fish protein hydrolysate, including acid hydrolysis, alkali hydrolysis, and enzymatic hydrolysis. It also explores the filtration process and purification methods used to isolate bioactive peptides. Furthermore, the article investigates the potential application of these peptides in the nutraceutical industry, particularly concerning non-communicable diseases.
2 Bioactive peptides from fish and fish byproducts
Underutilized fish as well as fishery wastes have limited customer preference because of their small size, physical appearance, texture, and smell. The utilization of underutilized or by-catch fish through the implementation of Fish-derived bioactive peptides technology has been acknowledged as an efficacious approach [32].
2.1 Chemical process
The cleavage of bonds is achieved by the utilization of strong acids or alkali under elevated temperatures. This strategy has been frequently employed in the past for the industry since it is economical as well as easy to implement [33]. However, this method has numerous limitations, such as being a tough process to regulate and the trend to provide changed amino acids. Fish-derived bioactive peptides may reduce their bioactive properties because of this adverse condition; thus the chemical methods have limited applications like nutritional incorporation, fertilizer, flavour and taste enhancers [34, 35]. The prevalence of acid hydrolysis exceeds that of the alkali method. Acid hydrolysis is an industrial method for the preparation of fish protein hydrolysate using strong acid (HCl, H2SO4) under high pressure and temperature for a long time, resulting in extensive hydrolysis of a substrate [36]. However, the major problem with acid hydrolysis is the destruction of tryptophan and high salt formation during neutralization [33, 37]. Phosphoric acid (H3PO4), hydrochloric acid (HCl), nitric acid (HNO3), malic acid, oxalic acid and other acids have also been investigated. In the alkali method, calcium, sodium, or potassium hydroxide achieved the desired degree of hydrolysis at a lower temperature (25–55 °C) in a few hours [33]. The disadvantage of this process is the loss of amino acid content in hydrolysates such as lysine, arginine, cystine, serine, isoleucine, threonine and the development of residues such as lanthionine and lysinoalanine [38]. The solvent extraction method in which the addition of 25% HCl (0.4 M) to the 75% methanol–water extraction significantly improves the recovery of protein base compounds like putrescine and cadaverine from fish tissue [39]. The pH-shift method is used to extract and recover fish muscle proteins, specifically for Atlantic croaker. The acid-aided process was found to have higher protein recoveries than the alkali-aided process [40]. Fish protein hydrolysates have favourable antioxidative properties and possess a strong capacity to inhibit ACE (Angiotensin-converting-enzyme), hence positioning them as a promising bioactive constituent for incorporation into food products [41]. Proteins were separated into different fractions using both acidic (HCl, pH 2.5) and alkaline (NaOH, pH 11.5) conditions. The resulting fractions had higher essential to non-essential amino acid ratios than those produced using enzymatic hydrolysis [42]. Several different species like silver carp [43], baltic herring and roach [44], bigeye snapper [45] and broadhead catfish and african catfish [46].
2.2 Enzymatic process
The use of enzymatic processes on several biopolymers found in food, including polysaccharides, proteins, and pectin, has the potential to enhance the overall quality of the product in terms of its physical, chemical, and sensory attributes [47]. The enzymatic extraction of proteins is conducted under highly controlled pH conditions to ensure that their nutritional properties remain intact. This retention of nutritional qualities is crucial for facilitating their broad adoption in the food industry. These applications include the production of milk substitutes [48], the stabilization of beverages, the enhancement of flavours in confectionery products [49], the development of protein supplements, and the manufacturing of animal feed and bacterial media [50,51,52]. Fish-derived bioactive peptides are gaining recognition for their diverse range of bioactive qualities which includes anti-microbial [30] antioxidant [28,29,30, 53], anti-inflammatory [30] and hormone-regulating properties [31].
Commercial enzymes utilized in the production of fish protein hydrolysate may originate from many sources: There are three main categories of proteolytic enzymes often used in various applications: microbial sources, plant sources, and animal sources. Microbial sources comprise enzymes like flavourzyme, alcalase, neutrase, umamizyme, and protamex. Plant sources include enzymes such as bromelain, ficin, and papain. Lastly, animal sources comprise enzymes like trypsin, pepsin, and chymotrypsin [54]. The significance of enzyme specificity relies on the amino acid sequence that bonds desired for cleavage [26, 55]. The protein sequences and size of the hydrolyzed peptides generated are influenced by the hydrolysis conditions and specificity, which play a significant role in determining the bioactivities of the hydrolysate. There is a possibility that changes in enzyme type, time, enzyme-to-substrate ratio, pH, temperature, solid-to-liquid ratio, and enzyme quantity provide diverse biological activity due to the production of different peptides [15].
3 Purification of bioactive peptide
Although bioactive peptides have been shown to have psychological advantages, their commercial utility is limited due to limitations in efficient purification. Fish hydrolysate combination is a complex mixture of bioactive peptides and several non-bioactive hydrolysed compounds. It is difficult to separate peptide fragments since they all have different sizes, charges, and physicochemical properties [15]. Utilising chromatography methods, biologically active peptides are usually segregated based on their molecular size, ionic charge, and differential affinity for the stationary and mobile phases [56, 57]. To acquire desired peptides, those approaches remove the harmful residue and unwanted solvents. Different effective purification methods have unique benefits as well as drawbacks depending on the applications. The commonly used techniques include Size extrusion chromatography, ion-exchange chromatography, membrane filtration including ultrafiltration and nanofiltration (NF), and reverse-phase high-pressure chromatography (RP-HPLC) [58].
3.1 Membrane filtration
A membrane is a narrow barrier with selective permeability that divides two areas with different chemical compositions [59]. Electrical fields, pressure, vacuum, and concentration can all be utilized as regulating factors in the filtration process to separate distinct components of a mixture according to their size, charge, or other qualities [60]. In comparison to conventional techniques like chromatography, this enables the purification of peptides with less energy consumption and without the need for solvents or other additives. Peptide structure and molecular weight distribution determine their bioactivities. Depending on their molecular size, peptides are frequently extracted from crude and raw hydrolysates using ultrafiltration (UF). Using membranes with molecular weight cut-off values of 3.5, 5, and 10 kDa, the tuna milt hydrolysate (TMH) was ultrafiltered to produce four separate fractions: TMH-I (molecular weight less than 3.5 kDa), TMH-II (molecular weight between 3.5 and 5 kDa), TMH-III (molecular weight between 5 and 10 kDa), and TMH-IV (molecular weight greater than 10 kDa). Compared to the other three fractions, the TMH-I fraction showed significantly greater levels of FRAP (ferric-reducing ability), ABTS (2,2-azino-bis-3-ethylbenzothiazoline-6-sulphonic acid), and DPPH (2,2-diphenyl-1-picrylhydrazyl) (P < 0.05) [61]. Peptides with a molecular weight of 3 kDa that were obtained from the meat protein hydrolysate of red-bellied pacu (Piaractus brachypomus) were ultrafiltered and their antioxidant activity was divided into various fractions. Several antioxidant tests, such as DPPH, FRAP, ABTS, and Fe2+ chelating activity, demonstrated that the ultrafiltered protein hydrolysate (RPMPH-IF) (MW < 3 kDa) fraction performed better than the crude hydrolysate in terms of antioxidant activity [62]. The crude peptides were separated using ultrafiltration membranes with a 5 kDa cut-off size, yielding two different fractions: F1, which contained peptides with a molecular weight less than 5 kDa, and F2, which contained peptides with a molecular weight greater than 5 kDa. The crude peptides, F1 and F2 were tested for their angiotensin-converting enzyme (ACE) activity at various concentrations between 0.5 and 5.0 mg/mL. According to the findings, the IC50 values for crude hydrolysate, F1 and F2 are 1811.00 μM, 963.00 μM, and 3800.00 μM [63]. The study result demonstrates the improved anti-hypertensive, anti-proliferative, and anti-diabetic effects of the peptides with reduced relative molecular weights.
3.2 Gel filtration chromatography
Molecules are separated according to their sizes using a technique called gel filtration chromatography (GFC), also known as size-exclusion chromatography (SEC) or molecular exclusion chromatography [64]. Depending on the application, a Millipore transmembrane with different pore sizes allows ultrafiltrated fractionates to flow through. To produce bioactive compounds with reduced molecular size, this technique makes use of various resin types, including Sephadex G-25 (whose molecular weight ranges from 10 to 5 kDa), Sephadex G-15 (whose molecular weight is below 1.5 kDa), and Sephadex G-10 (whose molecular weight is below 0.7 kDa) [26]. The active peaks obtained after the gel filtration of seela fish hydrolysates could efficiently remove 2,2-diphenyl-1-picryhydrazyl and hydroxyl radicals with percentages of 61.0 ± 2.3% and 58.7 ± 2.3%, respectively [65]. In a similar vein, the two active peaks for ribbon fish hydrolysate after gel filtration showed scavenging capacities of 60.0 ± 2.6% and 55.6 ± 1.8% [65]. The hydrolysate of round scad was divided into four distinct fractions (A, B, C, and D) using gel filtration chromatography using A Sephadex G-15 column (2.0 × 40 cm). Among the fractions, Fraction B exhibited the highest DPPH radical scavenging activity at 59.77 ± 1.24% [66]. Salmon bone hydrolysate was purified by ultrafiltration (< 0.65 and gel filtration chromatography, a fraction (G1) was found higher inhibitory effect against nitric oxide (NO). The fraction exhibited reducing activity on the expression of cyclooxygenase-2 (COX-2) mRNA, interleukin-6 (IL-6), nitric oxide synthase (iNOS), tumor necrosis factor-alpha (TNF-α) in RAW 264.7 cells, and nitric oxide (NO) produced by lipopolysaccharide (LPS) [67]. Skipjack tuna (Katsuwonus pelamis) head hydrolysate was purified using the Sephadex G-25 column. GC-1, GC-2, and GC-3 are the three active fractions collected from that GC-3 had higher activity in the DPPH radical scavenging assay, as seen by its lower EC50 value of 1.65 mg protein/mL. GC-1 and GC-2, the other two active components, had EC50 values of 3.49 and 5.73 mg protein/mL, respectively [68]. Bioactive peptides from aquatic by-products such as salmon [69], sardinella [70], skipjack tuna [71], and miiuy croaker [72] have been separated using the gel filtering approach. This study's conclusions show that peptide components with smaller average molecular weights have stronger antioxidants and other bioactive characteristics.
3.3 RP-HPLC
Reversed-phase high-performance liquid chromatography (RP-HPLC) is a commonly employed method for the purification of peptides, taking advantage of their hydrophobic properties. However, this technique has some drawbacks such as the requirement for large volumes of organic solvents, which creates environmental problems as well as long purification times and low yields which can enhance the production costs [73]. A set of nine peptides was successfully isolated from the round scad through the application of RP-HPLC. Among these peptides, the P3 fraction obtained from the hydrolysate exhibited the highest level of activity, as indicated by its IC50 value of 0.72 mg/mL towards ABTS radical. This peptide with a molecular weight of 302.74 Da contains the amino acids glycine, histidine and alanine. On the other hand, the P5 peptide (with a molecular weight of 282.13 Da) was obtained and demonstrated an IC50 value of 0.89 mg/mL. The amino acids profiling of this peptide included valine, glycine, and asparagine. [74]. The hydrolysates produced from the Alaska Pollack skins by the use of trypsin and Alcalase enzymes showed ACE inhibitory activity. The fish protein hydrolysate separated using RP-HPLC showed the amino acid sequence of PLGVP fraction with the highest level of ACE inhibitory activity, as evidenced by an IC50 value of 105.8 µM [75]. Purified peptides showed good antioxidant, anti-hypertensive and anti-diabetic properties as compared to crude hydrolysate.
4 Structure identification of bioactive peptide
The structural identification of bioactive peptides is specified by the amino acid sequence, after the purification of bioactive peptides [76]. Mass spectrometry is a susceptible and precise technique for determining molecular weight and elemental composition, owing to its ultrahigh specificity, accuracy, and rapidity [15]. It provides insights into the positive ions that are generated during ionization, which are correlated with the molecular structure and bond type [77]. MALDI-TOF MS (matrix-assisted laser desorption ionization-time of flight mass spectrometry), Ultra-high performance liquid chromatography (UHPLC) and Liquid chromatography coupled to mass spectrometry (LC–MS) are emerging techniques utilized for the sequencing of peptides [78, 79].
4.1 Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF–MS)
High-throughput matrix-assisted laser desorption/ionization (MALDI) technology compares the protein fingerprint with a library of reference spectra using a variety of algorithms built into systems [80]. Frequently, MALDI is used in conjunction with a TOF analyzer to determine the mass of intact peptides because it produces little to no fragmentation and makes it possible to identify the molecular ions of analytes even in complex mixtures of biopolymers [81]. Over time, MALDI-TOF-MS has shown to be a rather flexible method for analysing biological materials, particularly those including proteins and peptides. The skipjack tuna (Katsuwonus pelamis) protein head hydrolysate was detected using Q-TOF MS after being purified by ultrafiltration and reverse phase- high-pressure liquid chromatography. The extracted peptides amino acid sequences were SP, VDRYF, VHGVV, YE, FEM and FWRV with molecular weights of 202.3, 698.9, 509.7, 310.4, 425.6, and 606.8 Da. Excellent angiotensin inhibitory activity was shown in an IC50 value of 0.06, 0.28, 0.90, 0.80, 2.18 and 0.76. Especially SP and VDRYF are beneficial components for functional food against hypertension and cardiovascular diseases [82]. MALDI-TOF/TOF was used to identify the ACE inhibitory amino acid sequence of RGVGPVPAA (IC50 = 0.20 mg/ml) from the hydrolysate of shortfin scad waste [83]. This method has become an option for characterising proteins because of its resilience, capacity to ionise intact proteins, and tolerance for the presence of impurities [84]
4.2 Ultra-high performance liquid chromatography (UHPLC)
Ultra-high performance liquid chromatography (UHPLC) has shown effective in the analysis of complex mixtures in both isocratic and gradient modes used in various fields [85]. For material analysis, UHPLC offers additional benefits such as improved selectivity, sensitivity, and high throughput when paired with mass spectrometry (MS). UHPLC combined with tandem MS is very useful for both targeted and untargeted studies [86]. Due to its rapid separation capabilities, low solvent usage, high capacity, resolution, sensitivity, specificity, and selectivity, as well as its capacity to detect multiple ions through selective ion fragmentation, the UHPLC–ESI–MS/MS method has recently become a powerful tool for simultaneously determining bioactive components in food [87]. One popular ionisation technique used in many different protein science research approaches is electrospray ionisation (ESI). The molecular mass of polypeptides and other structural characteristics, such as amino acid sequences in complex materials, may be found using ESI spectrometry [88]. A potent ACE-inhibiting peptide (PAGPRGPA; IC50:7.90 μM)) was successfully identified from a three-spot seahorse protein by using ESI–MS MS [89]. The molecular weights and amino acid sequences of the four ACE inhibitory peptides (SSSKAKKMP, HGEGGRSTHE, WLGHGGRPDHE, and WRMDIDGDIMISEQEAHQR) were isolated from deep-water pink shrimp (Parapenaeus longirostris) determined using ESI–MS and ESI–MS/MS methods [90]. Furthermore, the introduction of ultra-high-performance liquid chromatography high-resolution mass spectrometry (UHPLC–HRMS) aims to tackle the complicated and extensive coverage of food bioactive proteins and peptides. A large variety of metabolites may be found and identified using this technology since it combines flexible and effective separation with high-sensitivity detection by HRMS [91].
4.3 Liquid chromatography coupled to mass spectrometry (LC–MS)
Bioactive proteins and peptides can be identified and quantified using liquid chromatography coupled with mass spectrometry (LC–MS) [84]. Based on this strategy, several approaches have emerged and been documented in recent years; they range from non-targeted exploratory analysis to specific procedures, depending upon the objective. While investigations make it easier to identify and quantify certain bioactive peptides, non-targeted analyses aim to characterize the proteomic profile of the sample, while targeted analyses facilitate the detection of specific bioactive peptides, enabling their quantification [88]. Liquid chromatography-mass spectrometry is the most promising approach for verifying the presence of peptides in food because of its great sensitivity and capacity to identify even minimal levels of peptides in complex matrices [84]. Compared to other chromatographic techniques, liquid chromatography techniques alone might not be a comprehensive solution for identifying and quantifying bioactive proteins and peptides; however, LC–MS in conjunction with tandem mass spectrometry has shown to be especially useful for profiling bioactive peptides with minimal preparative steps. LC–MS/MS was used for the identification of antioxidant peptides from mackerel (Scomber japonicus) muscle protein hydrolysates. Peptide sequence (ALSTWTLQLGSTSFSASPM) showed the highest (p < 0.05) DPPH scavenging activity (36.34 ± 4.64%) and another peptide (LGTLLFIAIPI) exhibited the highest (p < 0.05) SOD-like activity (28.94 ± 4.19%) [92]. Peptides derived from sturgeon were identified through high-performance liquid chromatography-tandem mass spectrometry. Among these, GDRESGPA (P1) displayed the most potent DPPH radical scavenging activity with an IC50 value of 1.93 mmol L−1. GPAGERGEGGPR (P11), exhibited the strongest DPP-IV inhibitory activity with an IC50 value of 2.14 mmol L−1. Additionally, GPPGADGQAGAK(P6) demonstrated the highest ACE inhibitory activity, with an IC50 value of 3.77 mmol L−1 [93].
5 Bioactive properties of fish-derived bioactive peptides in respective to non-communicable disease (NCDS)
5.1 Anti-proliferative fish bioactive peptides
Cancer is the second leading cause of mortality on a global scale resulting in an estimated 9.9 million deaths in 2020. The number of new cancer cases (incidence) increased by 26% and the number of cancer deaths increased by 21% between 2010 and 2019 [6]. Cancer is a class of illnesses distinguished by uncontrolled cell division and aberrant cell growth [94]. DNA mutations disturb the regulatory mechanism, resulting in a malignant tumor. Cancer progresses via three stages: initiation, promotion, and progression. Gene mutations initiate the process resulting in the unregulated regulation of biochemical signaling pathways. Pre-neoplastic cells accumulate during promotion, and genetic and phenotypic alterations occur during progression, resulting in rapid tumour development [94, 95]. The conventional approach to cancer treatment frequently involves a combination of surgical intervention, chemotherapy and radiation therapy. Nowadays, the field of nanotechnology has emerged as a valuable tool in enhancing the precision of tumor imaging, hence contributing to the overall efficacy of cancer treatment [96]. Nevertheless, conventional anti-cancer medications frequently exhibit a deficiency in distinguishing between cancerous and healthy cells, resulting in systemic toxicity and the occurrence of undesirable side effects. The utilization of sophisticated methodologies and pharmaceutical agents faces substantial costs and is accompanied by the potential for adverse effects on the kidneys, nervous system, cardiovascular system, and reproductive system [97,98,99].
Some natural compounds show good anti-cancerous effects and recent studies showed their effects in various in vitro and in vivo models [100, 101]. Bioactive peptides offer the potential to formulate drugs for cancer therapy. Generally, resources like plants and animals are used for producing bioactive peptides. Several studies showed fishery sources are the most beneficial for developing antiproliferative and antioxidant peptides (Tables 1 and 2). The use of fish by-product hydrolysates has shown great potential as a viable source of antioxidant peptides [102,103,104]. The investigation of eel protein hydrolysis (EPH) utilizing alcalase enzyme showed promising attributes in terms of antioxidative and anti-carcinogenic properties. The inhibition of MCF-7 (Michigan Cancer Foundation-7) cells was shown to be strongest in the treatment including 3 kDa EPH, in comparison to the treatments involving crude, 10 kDa, and 5 kDa EPH. The IC50 values for the crude, 3 kDa 5 kDa, 10 kDa, EPH were determined to be 21.50 µg/ml, 6.50 µg/ml, 11.08 µg/ml and 16.84 µg/ml respectively. The results presented in this study indicate that the 3 kDa EPH had the greatest efficacy in inhibiting MCF-7 cells [109]. Hydrolysis shortens amino acid chains and exposes more hydrophobic amino acids, improving antioxidative and anti-proliferative activities. The hydrolytic degradation of EPH resulted in the increased exposure of hydrophobic amino acids, namely isoleucine, methionine asparagine, phenylalanine, valine, and glutamine in the N-terminal region. This phenomenon perhaps contributes to the suppression of MCF-7 cancer cell lines [110].
The utilization of a protein hydrolysate derived from tuna trimmings (Thunnas albacares) in conjunction with 5-fluorouracil (30 mg/kg) has been shown to improve the rate of tumour suppression, alleviate the mucosal damage caused by 5-FU in the intestines, and retain the typical structure of the villi and crypt walls in the mucosa of the small intestine [111]. The peptide with anti-cancerous action is opposed to human prostate cancer PC-3 cells derived from anchovy peptic hydrolysates. The peptide designated as YALPAH demonstrated the most apparent positive charge and displayed the most potent anti-proliferative action, as seen by an IC50 value of 8.1 mg/ml [112]. Ultrafiltered roe hydrolysates (URH) prepared from giant grouper can suppress the growth of oral cancer cell lines (Ca9-22 and CAL 27). URH also caused the oral cancer cells to endure apoptosis, which is a programmed cell death process. The characteristics of apoptosis induced by URH include changes in cell morphology, accretion of cells in the sub-G1 stage of the cell cycle and increased expression of annexin V and PI [113]. The PAH 2.5 fraction obtained using ultrafiltration with a cutoff of > 2.5 kDa, exhibited the highest level of anti-proliferative activity (IC50: 1.39 mg/mL). Tuna cooking liquid possesses significant potential as a protein source to produce anti-proliferative peptides targeting MCF-7 cells. Its treatment with the cancer cell line resulted in cell cycle arrest specifically in the S phase and triggered apoptosis in MCF-7 cells [100]. Fish-derived bioactive peptides inhibit apoptosis in oral cancer cells via a process involving the production of reactive oxygen species (ROS) and superoxide, as well as mitochondrial polarization. These findings suggest that fish-derived bioactive peptides have a promising compound to be used as an apoptosis-based anti-cancer therapy for oral cancer.
5.2 Anti-hypertensive fish bioactive peptides
Hypertension is a chronic medical illness characterized by persistently elevated blood pressure in the arteries. CVDs (cardiovascular diseases) accounted for 20.5 million deaths and over 500 million people are affected worldwide in 2021 [6]. The Renin-Angiotensin System (RAS) is crucial for maintaining blood flow and homeostasis by regulating salt balance [117]. Angiotensin Converting Enzyme (ACE) catalyzes a specific reaction: converting Angiotensin-I to Angiotensin-II, which regulates blood pressure through vasoconstriction and salt retention. Inactivation and reduction of ACE is considered a significant mode of treatment for hypertension [118, 119]. Mostly ACE inhibitors, angiotensin receptor blockers and anti-hypertensive drugs (lisinopril, benazepril, captopril chlorthalidone and hydrochlorothiazide) are available in the market to treat hypertension [120]. But those drugs cause side effects because of that natural marine-based compounds come into the study.
A novel ACE-inhibitory peptide (GPLGVP; IC50 = 105.8 µM) was identified from Alaska Pollack skin protein hydrolysates, showing promising potential for blood pressure regulation [75].
The highly effective ACEi protein hydrolysate (TMPH) from skipjack tuna muscle was created using alcalase under optimal conditions. This resulted in an ACEi activity of 72.71% at a concentration of 1.0 mg/mL. Following this, six novel ACEi peptides were isolated from TMPH using ultrafiltration and chromatography techniques. These peptides were identified as Ser-Pro (SP), Val-Asp-Arg-Tyr-Phe (VDRYF), Val-His-Gly-Val-Val (VHGVV), Tyr-Glu (YE), Phe-Glu-Met (FEM), and Phe-Trp-Arg-Val (FWRV). Notably, SP and VDRYF exhibited significant ACEi activity, with IC50 values of 0.06 ± 0.01 and 0.28 ± 0.03 mg/mL [82]. The production of bioactive peptides from shortfin scad fish waste. The study includes purification and characterization of the peptides, as well as molecular docking studies to understand their interactions with the ACE enzyme. The isolated peptide sequence and its biological activity are determined. The study reveals that the purified peptide (GVGPVPAA) acts as a competitive inhibitor of ACE and has strong potential as an antihypertensive agent [83]. The hydrolysate was protein seahorse protein fractionated by dialysis, Sephadex G-25 gel filtration chromatography, and reverse-phase high-performance liquid chromatography. After consecutive purification, a potent ACE-inhibiting peptide composed of 8 amino acids (Pro-Ala-Gly-Pro-Arg-Gly-Pro-Ala; MW: 721.39 Da; IC50 value: 7.90 μM) [89]. Sturgeon skin protein extract hydrolyzed by flavourzyme exhibited angiotensin converting enzyme (ACE) inhibitory activity. The sequences of peptides from flavourzyme hydrolysates were identified using high-performance liquid chromatography-tandem mass spectrometry. Gly-Pro-Pro-Gly-Ala-Asp-Gly-Gln-Ala-Gly-Ala-Lys (P6) displayed the highest ACE inhibitory activity (ACE IC50 = 3.77 mmol L−1). The molecular docking analysis revealed that ACE inhibition by P6 is mainly attributed to strong hydrogen bonds [93]. The lizard fish protein hydrolysates with the amino acid sequence Val-Tyr-Pro which has the potential to block ACE activity. The results of this study indicate that muscle protein derived from lizard fish exhibits the potential of ACE inhibitory peptides [121]. The study demonstrated the presence of ACE inhibitory peptides in the muscle protein of seaweed pipefish. A total of four fractions were isolated by alcalase hydrolysates (Fr3-I, Fr3-II, Fr3-III and Fr3-IV). Among these fractions, Fr3-II and Fr3-III exhibit the most significant ACE inhibitory activity. The peptides included in these fractions exhibit negligible cytotoxicity towards human lung fibroblast cell lines, indicating their potential use as components with anti-hypertensive properties in multifunctional food products [122].
The remarkable ACE inhibitory peptides are produced from various fish species like Alaska pollack [75], deep-water pink shrimp [90], shark [123], ribbon fish [124], hound [125], tuna [126], krill [127], boar [128], pacific cod [129], grass carp [130], sardinelle [131], bighead carp [132] and kawakawa [133] also have been studied in respect of the ACE inhibitory bioactive peptides (Table 3).
The anti-hypertensive efficacy of lower molecular weight derived from enzymatically hydrolyzed fish protein fractionations was shown to be greater. The enhanced ACE inhibitory efficacy of peptides can be attributed to the inclusion of valine and arginine residues at the C-terminal. Consequently, the utilization of enzymes such as trypsin, which selectively cleave arginine may potentially facilitate the production of peptides with improved ACE inhibitory properties. The promise of bio-active peptides produced from fish as nutraceuticals and medicines lies in their efficacy in the prevention and treatment of hypertension.
5.3 Anti-diabetic fish bioactive peptides
Diabetes mellitus (DM) is a persistent metabolic disorder that impacts globally and its distinguished by elevated levels of blood glucose (hyperglycemia). Diabetes mellitus (DM) is commonly categorized into two primary classifications: type I diabetes (T1DM) and type II diabetes (T2DM) [134]. Insulin-dependent type I diabetes mellitus constitutes 10% of the total cases of diabetes mellitus, whereas non-insulin-dependent type II diabetes mellitus accounts for the remaining 90% of cases. Research findings indicate that the global prevalence of diabetes is projected to reach around 600 million cases by the year 2035 [135]. Hormone-like insulin is produced in the pancreas that regulates blood glucose levels. Insufficient insulin or insulin resistance results in abnormal blood glucose levels [136]. Fish-derived proteins and peptides have been shown to have anti-diabetic effects through various mechanisms, including stimulating glucagon-like peptide 1 (GLP-1) secretion, increasing insulin release, decline in dipeptidyl peptidase-IV (DPP-IV) activity, increasing glucose uptake, declining blood glucose concentrations, and upregulating glucose transporter type 4 (GLUT4) and peroxisome proliferator-activated receptor alpha (PPAR- α) [137,138,139] (Table 4). Peptides that inhibit DPP-IV are obtained from fish sources and typically consist of 3–15 amino acids. The most often occurring amino acid residues in these peptides are leucine, proline, valine, glycine, isoleucine, and phenylalanine [140, 141]. The protein hydrolysate was separated into four sub-fractions using RP-HPLC. The findings of the study indicated that the fourth sub-fraction (SF4) had the most potent inhibitory effect against DPP-IV, as evidenced by its IC50 value of 0.21 mg/mL [142].
Antarctic krill protein contains two peptides (AP and IPA) that inhibit DPP-IV, an enzyme that breaks down incretin hormones. Incretin hormones stimulate insulin secretion and reduce glucagon secretion, which helps to improve glucose control [143]. The administration of marine peptides demonstrated enhanced glucose digestion and increased insulin sensitivity in rats with type 2 diabetes mellitus (T2DM). The observed benefits may be attributed to the peptides capacity to reduce the effects of inflammation and oxidative stress as well as enhance the expression of GLUT4 and PPAR-α, both of which play crucial roles in glucose absorption and metabolism [139]. The hydrolysate derived from silver carp by the application of neutrase for five hours exhibited the most pronounced inhibitory action against dipeptidyl peptidase IV (DPP-IV). This inhibitory effect was seen to be at its peak with an inhibition rate of 81% when the hydrolysate was present at a level of 5 mg/mL. The peptide WGDEHIPGSPYH had the highest potency as a DPP-IV inhibitor, displaying an uncompetitive inhibition mechanism with an IC50 value of 0.35 mM [140]. The sardine protein was subjected to enzymatic treatment using a mixture of three enzymes (subtilisin, trypsin and flavourzyme to produce hydrolysates with antidiabetic activity. This hydrolysate was subsequently purified by size exclusion chromatography. The highest dipeptidyl peptidase IV inhibitory activity was obtained with an IC50 of 1.83 ± 0.05 mg/ml with molecular weight in the range of 800 to 1400 Da [141]. Blue whiting protein hydrolysate was produced using alcalase and flavourzyme and its simulated gastrointestinal digestion (SGID) sample was assessed for antidiabetic potential. The results demonstrate that the blue whiting protein hydrolysate had significant metabolic effects relevant to glucose control [144]. The anti-obesity peptides were generated from fish water-soluble protein by enzymatic conditions and optimized with the aid of response surface methodology. The porcine pancreas lipase and α-amylase inhibitory rate could reach 53.04 ± 1.32% and 20.03 ± 0.89%, while predicted values were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively [145]. The novel antidiabetic peptides were identified from the Chinese giant salamander (Andrias davidianus) protein hydrolysate. The peptides’ amino acid sequences were Cys-Ser-Ser-Val (MW = 393.99 Da), Tyr-Ser-Phe-Arg (MW = 570.99 Da), Ser-Ala-Ala-Pro (MW = 343.89 Da), Pro-Gly-Gly-Pro (MW = 325.99 Da) and Leu-Gly-Gly-Gly-Asn (MW = 415.99 Da) possessing α-amylase inhibitory activity IC50 of 13.76 × 103, 10.82 × 103, 4.46 × 103, 4.23 × 103, and 2.86 × 103 µg/mL, respectively; and for α-glucosidase with IC50 of 206.00, 162.00, 66.90, 63.50, and 42.93 µg/mL, respectively. The peptide LGGGN showed higher inhibition on both α-amylase and α-glucosidase and could be considered as a potential anti-diabetic inhibition [146]. The peptides produced from various fishery sources like salmon [147], boarfish [148] and tilapia [149] show good anti-diabetic potential.
Several laboratory and clinical investigations have provided data indicating that separated peptides might be incorporated as components in nutritional supplements or functional foods. These peptides can effectively block dipeptidyl peptidase-IV (DPP-IV), preventing the deterioration of glucagon-like peptide-1 (GLP-1) and maintaining insulin production. Furthermore, it is worth noting that most clinical trials are carried out using limited sample sizes, a factor that hinders the ability to make conclusive recommendations on the efficacy of these bioactive substances in the treatment and management of T2DM. Hence, it is imperative to conduct additional studies using larger sample sizes to provide further validation of the anti-diabetic ability.
6 Challenges and future perspectives
Fish peptides exhibit numerous biological functions, delivering them a promising bioactive constituent for the food, nutraceutical, and nutritional supplement sectors. The commercial use of bioactive peptides has been limited due to high costs. enzyme cost, long process, bitterness limiting oral consumption, lack of process optimization for bioactive properties, no control over the specific molecular weight of peptide, lack of food safety data, poor understanding between protein structure and bioactivity, absence of sufficient evidence showcasing the practical implementation of food and nutritional items, insufficiency of robust human data to substantiate claims regarding their health benefits and safety, no clear legal regulation or guidelines regarding the dosage and safety related to different age groups.
However, strategies and research are needed to industrialize the fish bioactive peptides. The high cost of production could be reduced by using economical raw materials like by-products, underutilized and trash fish. Systematic design of experiments approaches to optimize process parameters for best quality attributes. Several innovative and environmentally friendly methods, such as ultrafiltration membrane reactor, high-pressure hydrostatic processing and pulsed electric field-assisted enzymatic hydrolysis have been examined to enhance the overall functionality and effectiveness of the process. Peptides own a bitter test that could change the taste of the final product so suitable methods like debittering, encapsulation or masking approaches are used to tackle that problem. Utilizing in silico methods has been identified as a highly effective way to identify and synthesize specific bioactive peptides. Research on stability, bioavailability, absorption, distribution, metabolism, and excretion withdrew the process of action and safety. In conclusion, the present amount of clinical research on the prospective biological activities and health benefits offered by fish peptides is limited, suggesting more human investigations to gain a comprehensive understanding of the physiological significance of these peptides.
7 Conclusion
The fish processing industry generates huge, untapped nutritional-rich material that can be converted into protein hydrolysate. Fish-derived bioactive peptides provide significant applications in pharmaceuticals, nutraceuticals and functional food ingredients industries. Bioactivities of peptides derived from fish show cardioprotective, anti-hypertensive, anti-cancer, anti-diabetic, and anti-oxidative effects, suggesting their promising potential in the treatments and preventive care for NCD. Further research is required to develop pharmaceutical applications and more understanding of the mechanisms of bioavailability and bioaccessibility of fish-derived bioactive peptides.
Data availability
All data generated or analyzed during this study are included in this article.
Code availability
Not applicable.
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The authors acknowledge the Director, ICAR-CIFT and Kerala University of Fisheries and Ocean Studies for providing the facilities.
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RB collected the literature and drafted the manuscript with the support of PP and SKR. AR, EK, and RRSR edited and revised the manuscript. RV conceptualized, edited, and revised the manuscript. (Ravi Baraiya—RB; Prakash Patekar—PP; Sanjaykumar Rathod—SKR; Anandan R—AR; Elavarasan K—EK; Radhika Rajasree S R –RRSR & Renuka V –RV).
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Baraiya, R., Anandan, R., Elavarasan, K. et al. Potential of fish bioactive peptides for the prevention of global pandemic non-communicable disease: production, purification, identification, and health benefits. Discov Food 4, 34 (2024). https://doi.org/10.1007/s44187-024-00097-5
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DOI: https://doi.org/10.1007/s44187-024-00097-5