@article{Liu2026, 
author = {Yongqi Liu and Xiao  Hu and Shanggui Deng and Shengjun  Chen and Yongqiang  Zhao and Hui  Huang and Bo  Qi and Huan  Xiang and Xiaoshan   Long and Yifeng  Rang and Chengmei  Yin},
title = {Study on preparation and physicochemical properties of α-glucosidaseinhibitory peptide from Trachinotus Ovatus},
year = {2026},
journal = {South China Fisheries Science},
volume = {22},
number = {2},
pages = {227-236},
keywords = {Trachinotus ovatus, α-glucosidase Inhibitory peptide, Hpyerglycemic activity, Physicochemical property},
url = {https://www.sciopen.com/article/10.12131/20250282},
doi = {10.12131/20250282},
abstract = {Research on glucose-lowering peptides derived from marine organisms remains relatively limited, and systematic studies on α-glucosidase inhibitory peptides from Trachinotus ovatus are particularly scarce. This study aims to prepare α-glucosidase inhibitory peptide (AGIP) from T. ovatus and investigate their physicochemical properties, thereby laying a theoretical foundation for developing novel hypoglycemic functional foods and promoting the value-added utilization of T. ovatus by-products. We used T. ovatus as the raw material and adopted enzymatic hydrolysis to prepare AGIP. We screened the optimal protease and hydrolysis time based on the α-glucosidase (AG) inhibition rate and degree of hydrolysis (DH) as evaluation indices. Then we investigated the inhibition type, gastrointestinal digestive stability, thermal stability, and acid-base stability of AGIP through enzyme inhibition kinetics, and analyzed its molecular weight distribution and amino acid composition. The results show that the hydrolysate obtained with compound protease after 4 h of hydrolysis exhibited the highest AG inhibition rate of (58.66±0.75)%, with DH of (13.84±0.08)%. The half-maximal inhibitory concentration (IC50) of this hydrolysate toward AG was (20.41±1.75) mg·mL−1, and its inhibition against AG followed a mixed-type inhibition mechanism. After simulated gastrointestinal digestion, the AG inhibition rate of the hydrolysate further increased to 66.55%. The relative molecular mass of 94.14% of the hydrolysate components was below 3kDa, and the content of hydrophobic amino acids (Ala, Pro, Val, Met, Ile, Leu, Phe, and Trp) was relatively high. In conclusion, the α-glucosidase inhibitory peptides prepared in this study demonstrate favorable inhibitory activity and stability, which provides theoretical support for the high-value utilization of T. ovatus and the development of hypoglycemic functional foods.}
}