Evaluation of taste active peptides and amino acids from anchovy proteins in fish sauce by insilico approach.

Abstract

Enzymatic activity and microbial fermentation play a prominent role in the bioconversion of complex muscle tissue into smaller units of peptides and amino acids, possibly contribute to sensory properties. Thus, this study screens and evaluate anchovy proteins with taste-active peptides and amino acids by the reaction of multiple enzymes using an insilico approach. Information about sensory components was provided based on an insilico analysis using tools available in the BIOPEP-UWM database. Proteins from anchovy, namely myosin heavy chain 6 alpha, myosin light chain 1, cytochrome B, and NADH ubiquinone oxidoreductase, were subjected to insilico digestion with the combination of 23 enzymes. This led to the release of taste-active peptides and amino acids, including umami, sweet, salty, sour, and bitter sensory properties. The combination of multiple enzymes released a more significant number of taste-active peptides and amino acids for both myosins compared to other proteins.