Rainbow trout proteins as potential source of biologically active peptides
Journal Title: Medycyna Ogólna i Nauki o Zdrowiu - Year 2015, Vol 21, Issue 3
Abstract
Introduction and objective. Bioactive peptides derived from food proteins are considered as regulators of the cardiovascular, nervous, and digestive systems. Peptides with antihypertensive activity are the best recognized bioactive peptides, of which angiotensin I-converting enzyme inhibitors (ACE inhibitors) are the most known. The aim of presented study was to determine the profile of the potential biological activity of a selected rainbow trout (Oncorhynchus mykiss) protein using bioinformatics tools from the Bioactive Proteins and Peptides database – BIOPEP. Material and methods. Amino acid sequences of 7 proteins originated from trout meat tissue were taken from the UniProt database. The frequency of occurrence of bioactive fragments in protein sequence (parameter A) and potential biological activity of protein (parameter B) were determined for all selected proteins using a procedure built into the BIOPEP database. Then, in silico proteolysis was performed using 6 proteolytic enzymes, which acted separately. Results. It was found that the largest number of bioactive peptides sequences (1,999) was hidden in trout collagen, including the largest number of ACE inhibitors. Collagen was characterized by the highest value of the parameter A (0.7316) and B (0.1651) for fragments with ACE inhibitory activity. Ficin and papain released the largest number of bioactive fragments from the trout proteins tested. Conclusions. Based on these results, it can be concluded that collagen is the richest source of bioactive peptides when compared with the trout proteins studied. Ficin and papain can be used to produce hydrolysates or peptides with potential biological activity from trout meat tissue.key words: trout, bioactive peptides, ACE inhibitors,[i] in silico[/i] hydrolysis
Authors and Affiliations
Monika Pliszka, Justyna Borawska, Małgorzata Darewicz
Keywords
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- EP ID EP79472
- DOI 10.5604/20834543.1165361
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