【摘要】 目前关于海洋生物源降血糖肽的研究相对匮乏，针对卵形鲳鲹（Trachinotus ovatus）中α-葡萄糖苷酶抑制肽的系统性研究较少。本研究旨在制备卵形鲳鲹α-葡萄糖苷酶抑制肽（α-glucosidase inhibitory peptide, AGIP）并探究其理化特性，以期为开发新型降糖功能性食品及卵形鲳鲹副产物高值化利用提供理论依据。以卵形鲳鲹为原料，采用酶解法制备AGIP。以α-葡萄糖苷酶（α-glucosidase, AG）抑制率和水解度为评价指标筛选最适蛋白酶和酶解时间，通过酶抑制动力学探讨AGIP的抑制类型及其胃肠道消化稳定性、热稳定性、酸碱稳定性，分析其分子质量分布及氨基酸组成。结果显示，采用复合蛋白酶水解4 h所得产物的AG抑制率最高，为（58.66±0.75）%，水解度为（13.84±0.08）%；其半抑制浓度（IC50）为（20.41±1.75） mg·mL^-1，抑制作用为混合型抑制类型；该法制备所得的酶解产物经模拟胃肠道消化后，AG抑制率进一步提升至66.55%；酶解产物的分子质量低于3 kDa的组分占94.14%，且疏水性氨基酸（包括Ala、Pro、Val、Met、Ile、Leu、Phe和Trp）含量较高。本研究制备的卵形鲳鲹α-葡萄糖苷酶抑制肽具有良好的抑制活性及稳定性，可为卵形鲳鲹高值化利用及降糖功能食品开发提供理论支撑。更多还原

【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 byproducts. 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 3 kDa, 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.更多还原