Enzymatic hydrolysis and microbial fermentation: The most favorable biotechnological methods for the release of bioactive peptides
- PMID: 35415659
- PMCID: PMC8991988
- DOI: 10.1016/j.fochms.2021.100047
Enzymatic hydrolysis and microbial fermentation: The most favorable biotechnological methods for the release of bioactive peptides
Abstract
Bioactive peptides are biomolecules derived from proteins. They contain anywhere from 2 to 20 amino acids and have different bioactivities. For example, they have antihypertensive activity, antioxidant activity, antimicrobial activity, etc. However, bioactive peptides are encrypted and inactive in the parental protein, so it is necessary to release them to show their bioactivity. For this, there are different methods, where biotechnological methods are highly favorable, highlighting enzymatic hydrolysis and microbial fermentation. The choice of the method to be used depends on different factors, which is why it is essential to know about the process, its principle, and its advantages and disadvantages. The process of peptide release is critical to generate various peptide sequences, which will produce different biological effects in the hydrolysate. This review focuses on providing extensive information on the enzymatic method and microbial fermentation to facilitate selecting the method that provides the most benefits.
Keywords: Bioactive peptides; Biotechnology; Enzymatic hydrolysis; Microbial fermentation.
© 2021 The Author(s).
Conflict of interest statement
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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References
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- Acquah, C., Stefano, E. Di, & Udenigwe, C. C. (2018). Role of hydrophobicity in food peptide functionality and bioactivity. Journal of Food Bioactives, 4, 88–98. 10.31665/jfb.2018.4164.
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- Agyei, D., Ongkudon, C. M., Yi, C., Chan, A. S., & Danquah, M. K. (2016). Food and Bioproducts Processing Bioprocess challenges to the isolation and purification of bioactive peptides. 8, 244–246.
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