Abstract
Enzymes are the biocatalysts having a catalytic power that speeds up a chemical reaction without changing the equilibrium of the reaction. Almost all enzymes are protein in nature and the biocatalytic power lies in the integrity of their structural conformation. The enzymes are highly specific with their substrate molecules that convert into the product by decreasing the activation energy, without getting changed itself. However, the biocatalytic power of the enzymes also depends on several physico-chemical parameters such as temperature, pH, salt concentrations, etc. of the reaction. The enzyme catalysis can be quantitatively revealed by the enzyme kinetics mechanism which measures the reaction rates and the affinity of enzymes towards the substrates and inhibitors. The enzymes can be isolated from the various biological factories such as plant, animal, or microbial cells depending upon the type of enzyme. However, in order to produce at large scale, the microbial sources are the best choice which can effectively reduce the production and purification cost of enzymes. The enzymes are widely used in various sectors such as agriculture, environmental, leather tanning, paper and pulp, chemical and pharmaceutical, detergent, food and beverages, etc. In this chapter, we are mainly focussing on the role of enzymes in the food industry.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Barnes-Svarney, P., & Svarney, T. E. (2014). The handy biology answer book. Visible Ink Press.
Bisswanger, H. (2017). Enzyme kinetics: Principles and methods. John Wiley & Sons.
Boyce, S., & Tipton, K. F. (2001). Enzyme classification and nomenclature. eLS. https://doi.org/10.1038/npg.els.0000710
Dai, N., Schaffer, A. A., Petreikov, M., & Granot, D. (1995). Arabidopsis thaliana hexokinase cDNA isolated by complementation of yeast cells. Plant Physiology, 108(2), 879.
El Enshasy, H. A., Elsayed, E. A., Suhaimi, N., Abd Malek, R., & Esawy, M. (2018). Bioprocess optimization for pectinase production using Aspergillus niger in a submerged cultivation system. BMC Biotechnology, 18(1), 71.
Faulds, C. B., Mandalari, G., LoCurto, R., Bisignano, G., & Waldron, K. W. (2004). Arabinoxylan and mono-and dimeric ferulic acid release from brewer’s grain and wheat bran by feruloyl esterases and glycosyl hydrolases from humicolainsolens. Applied Microbiology and Biotechnology, 64(5), 644–650.
Gazel, N., & Yildiz, H. B. (2016). Enzyme-based biosensors in food industry via surface modifications. In Surface treatments for biological, chemical, and physical applications (pp. 227–252). Wiley.
Gramss, G., & Rudeschko, O. (1998). Activities of oxidoreductase enzymes in tissue extracts and sterile root exudates of three crop plants, and some properties of the peroxidase component. New Phytologist, 138(3), 401–409.
Heinstra, P. W., Geer, B. W., Seykens, D., & Langevin, M. (1989). The metabolism of ethanol-derived acetaldehyde by alcohol dehydrogenase (EC 1.1. 1.1) and aldehyde dehydrogenase (EC 1.2. 1.3) in Drosophila melanogaster larvae. Biochemical Journal, 259(3), 791–797.
Huang, S. K., Chiu, A. W. H., Pu, Y. S., Huang, Y. K., Chung, C. J., Tsai, H. J., et al. (2008). Arsenic methylation capability, heme oxygenase-1 and NADPH quinone oxidoreductase-1 genetic polymorphisms and the stage and grade of urothelial carcinomas. Urologia Internationalis, 80(4), 405–412.
Huhtanen, P., & Khalili, H. (1992). The effect of sucrose supplements on particle-associated carboxymethylcellulase (EC 3.2. 1.4) and xylanase (EC 3.2. 1.8) activities in cattle given grass-silage-based diet. British Journal of Nutrition, 67(2), 245–255.
Janeček, S. (2009). Amylolytic enzymes-focus on the alpha-amylases from archaea and plants. Nova Biotechnologica et Chimica, 9(1), 5–25.
Kiess, M., Hecht, H. J., & Kalisz, H. M. (1998). Glucose oxidase from Penicillium amagasakiense: Primary structure and comparison with other glucose-methanol-choline (GMC) oxidoreductases. European Journal of Biochemistry, 252(1), 90–99.
Kilcawley, K. N., Wilkinson, M. G., & Fox, P. F. (1998). Enzyme-modified cheese. International Dairy Journal, 8(1), 1–10.
Kohler, R. (1971). The background to Eduard Buchner’s discovery of cell-free fermentation. Journal of the History of Biology, 4, 35–61.
Kouker, G., & Jaeger, K. E. (1987). Specific and sensitive plate assay for bacterial lipases. Applied and Environmental Microbiology, 53(1), 211–213.
Kuhajda, F. P., et al. (2011). Pharmacological glycerol-3-phosphate acyltransferase inhibition decreases food intake and adiposity and increases insulin sensitivity in diet-induced obesity. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, 301(1), R116–R130.
Li, S., Yang, X., Yang, S., Zhu, M., & Wang, X. (2012). Technology prospecting on enzymes: Application, marketing and engineering. Computational and Structural Biotechnology Journal, 2(3), e201209017.
Marseglia, A., Castellazzi, A. M., Valsecchi, C., Licari, A., Piva, G., Rossi, F., Fiorentini, L., & Marseglia, G. L. (2013). Outcome of oral provocation test in egg-sensitive children receiving semi-fat hard cheese Grana Padano PDO (protected designation of origin) containing, or not, lysozyme. European Journal of Nutrition, 52(3), 877–883.
Martín, M. A., Ramos, S., Granado-Serrano, A. B., Rodríguez-Ramiro, I., Trujillo, M., Bravo, L., & Goya, L. (2010). Hydroxytyrosol induces antioxidant/detoxificant enzymes and Nrf2 translocation via extracellular regulated kinases and phosphatidylinositol-3-kinase/protein kinase B pathways in HepG2 cells. Molecular Nutrition & Food Research, 54(7), 956–966.
McComb, R. B., Bowers Jr, G. N., & Posen, S. (2013). Alkaline phosphatase. Springer Science & Business Media.
Morisseau, C., Schebb, N. H., Dong, H., Ulu, A., Aronov, P. A., & Hammock, B. D. (2012). Role of soluble epoxide hydrolase phosphatase activity in the metabolism of lysophosphatidic acids. Biochemical and Biophysical Research Communications, 419(4), 796–800.
Nandakumar, J., Nair, P. A., & Shuman, S. (2007). Last stop on the road to repair: Structure of E. coli DNA ligase bound to nicked DNA-adenylate. Molecular Cell, 26(2), 257–271.
Nawaz, M. A., Karim, A., Aman, A., Marchetti, R., Qader, S. A. U., & Molinaro, A. (2015). Continuous degradation of maltose: Improvement in stability and catalytic properties of maltase (α-glucosidase) through immobilization using agar-agar gel as a support. Bioprocess and Biosystems Engineering, 38(4), 631–638.
Orita, M., Yamamoto, S., Katayama, N., Aoki, M., Takayama, K., Yamagiwa, Y., & Takeuchi, M. (2001). Coumarin and chromen-4-one analogues as tautomerase inhibitors of macrophage migration inhibitory factor: Discovery and X-ray crystallography. Journal of Medicinal Chemistry, 44(4), 540–547.
Perrier, J., Durand, A., Giardina, T., & Puigserver, A. (2005). Catabolism of intracellular N-terminal acetylated proteins: Involvement of acylpeptide hydrolase and acylase. Biochimie, 87(8), 673–685.
Portevin, D., de Sousa-D’Auria, C., Montrozier, H., Houssin, C., Stella, A., Lanéelle, M. A., et al. (2005). The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth identification of the carboxylation product and determination of the ACYL-CoA carboxylase components. Journal of Biological Chemistry, 280(10), 8862–8874.
Pumirat, P., Vanaporn, M., Pinweha, P., Tandhavanant, S., Korbsrisate, S., & Chantratita, N. (2014). The role of short-chain dehydrogenase/oxidoreductase, induced by salt stress, on host interaction of B. pseudomallei. BMC Microbiology, 14(1), 1.
Punekar, N. S. (2018). Enzymes. Springer.
Rhimi, M., Haser, R., & Aghajari, N. (2008). Bacterial sucrose isomerases: Properties and structural studies. Biologia, 63(6), 1020.
Shibata, N., Tamagaki, H., Hieda, N., Akita, K., Komori, H., Shomura, Y., & Toraya, T. (2010). Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates. Journal of Biological Chemistry, 285(34), 26484–26493.
Shixian, Q., VanCrey, B., Shi, J., Kakuda, Y., & Jiang, Y. (2006). Green tea extract thermogenesis-induced weight loss by epigallocatechin gallate inhibition of catechol-O-methyltransferase. Journal of Medicinal Food, 9(4), 451–458.
Smit, B. A., Engels, W. J., & Smit, G. (2009). Branched chain aldehydes: Production and breakdown pathways and relevance for flavour in foods. Applied Microbiology and Biotechnology, 81(6), 987–999.
Souza, P. M. D. (2010). Application of microbial α-amylase in industry—A review. Brazilian Journal of Microbiology, 41(4), 850–861.
Staudigl, P., Haltrich, D., & Peterbauer, C. K. (2014). L-Arabinose isomerase and D-xylose isomerase from Lactobacillus reuteri: Characterization, coexpression in the food grade host Lactobacillus plantarum, and application in the conversion of D-galactose and D-glucose. Journal of Agricultural and Food Chemistry, 62(7), 1617–1624.
Tapre, A. R., & Jain, R. K. (2014). Pectinases: Enzymes for fruit processing industry. International Food Research Journal, 21(2), 447–453.
van der Werf, M. J., van den Tweel, W. J., Kamphuis, J., Hartmans, S., & de Bont, J. A. (1994). The potential of lyases for the industrial production of optically active compounds. Trends in Biotechnology, 12(3), 95–103.
Vanderlinde, R. E. (1985). Measurement of total lactate dehydrogenase activity. Annals of Clinical and Laboratory Science, 15(1), 13–31.
Vu, T. K. H., & Le, V. V. M. (2008). Biochemical studies on the immobilization of the enzyme invertase (EC. 3.2. 1.26) in alginate gel and its kinetics. ASEAN Food Journal, 15(1), 73–78.
Wilson, T. E., Grawunder, U., & Lieber, M. R. (1997). Yeast DNA ligase IV mediates non-homologous DNA end joining. Nature, 388(6641), 495–498.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2022 The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Khade, S.M., Srivastava, S.K., Kamble, L.H., Srivastava, J. (2022). Food Enzymes: General Properties and Kinetics. In: Dutt Tripathi, A., Darani, K.K., Srivastava, S.K. (eds) Novel Food Grade Enzymes . Springer, Singapore. https://doi.org/10.1007/978-981-19-1288-7_1
Download citation
DOI: https://doi.org/10.1007/978-981-19-1288-7_1
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-19-1287-0
Online ISBN: 978-981-19-1288-7
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)