Fish proteins as potential precursors of taste-active compounds: an in silico study.

Abstract

Fish protein is a good source of amino acids and peptides with sensory properties. Theoretically, the type of protein affects the taste quality of the protein hydrolysates. To better use fish protein in the food ingredients industry, an in silico approach was adopted to evaluate the potential of fish protein to release taste-active compounds. Six types of protein from seven commercial fishes were screened from the Uniprot knowledge base. The results showed that a remarkable number of umami fragments presented in myosin and parvalbumin (PB), such as glutamic acid (Glu), aspartic acid (Asp), and Asp- and Glu- containing peptides, whereas sweet amino acids and bitter peptides (e.g., Pro- and Gly- containing peptides) were mainly found in collagen (CGI) in all fish samples. After the in silico proteolysis by papain, a difference in the profile of taste-active fragments was observed among the six types of proteins. Amino acids were the main hydrolysis products of these proteins, especially umami, sweet, and bitter amino acids, significantly contributing to the taste formation of protein hydrolysates. Besides, the myosin and CGI hydrolysates were abundant in taste active peptides both in types and quantities. Myosin is a promising protein source for producing umami fragments, and CGI seems to be a good precursor of sweet and bitter fragments. Different types of protein have an essential effect on the taste of protein hydrolysates. © 2022 Society of Chemical Industry.