Antioxidative activities of hazelnut protein hydrolyzates as predicted by in silico analysis techniques

Abstract

Recently, a variety of studies have been carried out on the production and analysis of bioactive peptides. Here, based on in silico methods, antioxidative behavior of hazelnut (Corylus avellana L.) peptides, which could be prepared by enzymatic treatments with 3 gastrointestinal (GI) and 3 non-GI enzymes were evaluated. On 10/03/2017, UniProt database listed 469 hazelnut proteins. In the current study, a subset (23 ribosomal proteins) of these proteins were examined and the activity of the GI proteases (trypsin, pepsin, chymotrypsin) for the production of antioxidative peptides were compared to non-GI proteases (thermolysin, papain and bromelain). Firstly, potential antioxidative peptide sequences were determined. GI proteases were less effective compared to non-GI proteases in the manufacture of antioxidative peptides. Antioxidative property of peptides, which were obtained by thermolysin or papain treatments, were significantly higher compared to GI proteases. When all 23 proteins were treated 37 antioxidative peptides were formed by thermolysin, while 10 antioxidative peptides were predicted for trypsin. Of the 138 cases studied (23 proteins x 6 proteases), 44 antioxidative peptides were detected (i.e., 1 peptide in approx. 32% of all cases). Based on current findings, hazelnut proteins can be considered a valuable resource for antioxidative peptide manufacture.