LAUSR

BACKGROUND Fish protein is a good source to release amino acids and peptides with sensory properties. Theoretically, the type of protein affects the taste quality of the protein decomposed products. To better apply fish protein to the food ingredients industry, an in silico approach was used to evaluate the potential of fish protein to release taste-active compounds. RESULTS Six types of proteins from seven commercial fishes were screened from the Uniprot knowledgebase. The results showed that a remarkable number of umami fragments presented in myosin and parvalbumin, 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) was mainly found in collagen of all fish samples. After the in silico proteolysis by papain, a distinguished 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 types and quantities of taste active peptides were abundant in both myosin and collagen hydrolysates. CONCLUSION Myosin is a promising protein source for producing umami fragments, while collagen seems to be a good precursor of sweet and bitter fragments. Moreover, protein types have an essential effect on the taste of protein hydrolysates. This article is protected by copyright. All rights reserved.