State Key Laboratory of Food Science and Resources Jiangnan University||School of Food Science and Technology Jiangnan UniversitySchool of Food Science and Technology Jiangnan UniversitySchool of Food Science and Technology Jiangnan UniversitySchool of Food Science and Technology Jiangnan University||Science Center for Future Foods Jiangnan University||||||International Joint Laboratory for Food Safety Jiangnan University||;
School of Food Science and Technology Jiangnan University;
Science Center for Future Foods Jiangnan University||School of Food Science and Technology Jiangnan University||Jiaxing Institute of Future Food;
State Key Laboratory of Food Science and Resources Jiangnan University||Science Center for Future Foods Jiangnan University||School of Food Science and Technology Jiangnan University||International Joint Laboratory for Food Safety Jiangnan University;
? 2023Peptides in cheese flavoring produced through proteolysis plus fermentation generated bitterness. Bitterness of individual peptide can be quantified using quantitative structure–activity relationship, where molecular mass (M), hydrophobicity, residues, C-terminal hydrophobic amino acids (C-HAAs), and N-terminal basic ones (N-BAAs) are crucial. However, their accumulative influence on the overall bitterness of peptide mixture remains unknown. This study delved into extensive proteolysis to debitter and to correlate the multi-influencing factors of peptides and the collective bitterness. As hydrolysis increased from 7.5 % to 28.0 %, bitterness reduced from 5.0 to 0.3–2.7 scores, contingent on proteases used, in which FU was optimal. The overall bitterness cannot be predicted through the summation of individual peptide bitterness, which depended on M (0.5–3 kDa) and 5–23 residues, followed by N-BAAs and C-HAAs. Analysis of enzymatic cleavage sites and substrate characteristics revealed, to more effectively debitter bovine milk protein hydrolysates, proteases specifically cleaving Pro, Leu, Phe, and Val were desired.