Abstract
The application of limited hydrolysis on wheat gluten (WG) has been found to be a highly effective method for improving a wide range of functional properties associated with plant protein. However, the bitter peptides formed during this process have an unpleasant bitterness. To provide a theoretical framework for de-bittering techniques, this study examined the modulation of bitterness intensity in wheat gluten hydrolysates (WGHs) by manipulating enzyme cleavage sites and degree of hydrolysis (DH). It was found that the bitter peptide's release content increased significantly, and the bitterness threshold decreased markedly with increasing DH. Furthermore, the structure-bitterness threshold association of bitter peptides was investigated. The results indicated that peptide segments in molecular weights (MW) from 500 to 1000 exhibited the greatest influence on bitterness threshold compared to peptides with other MWs. The percentage of total hydrophobic amino acid content and position of some hydrophobic amino acids in the amino acid sequence had a significant effect on the bitterness threshold. Finally, 47 peptides were identified by high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) analysis. These peptides were mainly small peptides with less than 13 amino acid residues and MW below 1500 Da, and most of them had Q values higher than 5855 J/mol.
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