Bovine meat proteins as potential precursors of biologically active peptides - a computational study based on the BIOPEP database.

摘要

The aims of the present study were to perform an in silico evaluation of beef proteins as potential precursors of biologically active peptides and to determine whether such peptides can be released by selected proteolytic enzymes. The sequences of 19 beef proteins were processed using the BIOPEP database and programme. Profiles of potential biological activity of protein fragments were determined and the following parameters were calculated: the frequency of occurrence of fragments with given activity, the frequency of release of fragments with given activity by selected enzymes and the relative frequency of release of fragments with given activity by selected enzymes. Among the examined proteins, collagen and elastin appeared to be the richest potential source of bioactive peptides, in particular of angiotensin-converting enzyme inhibitors, antithrombotic fragments, inhibitors of dipeptidyl peptidase IV and peptides regulating gastric mucosal activity. The high number of bioactive fragments in collagen and elastin was associated with high contents of glycine and proline, amino acids that are most abundant in biologically active fragments. Of the 2 investigated proteolytic enzymes, Proteinase K, an enzyme with broad specificity (e.g. against peptide bonds formed by the carboxyl groups of proline) can release considerably more biologically active fragments than Proteinase P1, an enzyme with narrow specificity, not including proline residues.