详细信息
Optimization and Molecular Mechanism of Novel alpha-Glucosidase Inhibitory Peptides Derived from Camellia Seed Cake through Enzymatic Hydrolysis ( SCI-EXPANDED收录) 被引量:9
文献类型:期刊文献
英文题名:Optimization and Molecular Mechanism of Novel alpha-Glucosidase Inhibitory Peptides Derived from Camellia Seed Cake through Enzymatic Hydrolysis
作者:Zhang, Yuanping[1] Wu, Fenghua[1] He, Zhiping[1] Fang, Xuezhi[2] Liu, Xingquan[1]
第一作者:Zhang, Yuanping
通信作者:Liu, XQ[1]
机构:[1]Zhejiang Agr & Forestry Univ, Coll Food & Hlth, Hangzhou 311300, Peoples R China;[2]Chinese Acad Forestry, Res Inst Subtrop Forestry, Hangzhou 311400, Peoples R China
年份:2023
卷号:12
期号:2
外文期刊名:FOODS
收录:;Scopus(收录号:2-s2.0-85146810374);WOS:【SCI-EXPANDED(收录号:WOS:000918299700001)】;
基金:This research was funded by the key research and development program of Zhejiang Province (No. 2021C02014).
语种:英文
外文关键词:camellia seed cake protein (CSCP); alpha-glucosidase; Inhibition kinetic; molecular docking
摘要:In recent years, food-derived hypoglycemic peptides have received a lot of attention in the study of active peptides, but their anti-diabetic mechanism of action is not yet clear. In this study, camellia seed cake protein (CSCP) was used to prepare active peptides with alpha-glucosidase inhibition. The optimization of the preparation of camellia seed cake protein hydrolyzed peptides (CSCPH) was conducted via response surface methodology (RSM) using a protamex with alpha-glucosidase inhibition as an indicator. The optimal hydrolysis conditions were pH 7.11, 4300 U/g enzyme concentration, 50 C-? hydrolysis temperature, and 3.95 h hydrolysis time. Under these conditions, the alpha-glucosidase inhibition rate of CSCPH was 58.70% (IC50 8.442 +/- 0.33 mg/mL). The peptides with high alpha-glucosidase inhibitory activity were isolated from CSCPH by ultrafiltration and Sephadex G25. Leu-Leu-ValLeu-Tyr-Tyr-Glu-Tyr (LLVLYYEY) and Leu-Leu-Leu-Leu-Pro-Ser-Tyr-Ser-Glu-Phe (LLLLPSYSEF) were identified and synthesized for the first time by Liquid chromatography electrospray ionisation tandem mass spectrometry (LC-ESI-MS/MS) analysis and virtual screening with IC50 values of 0.33 and 1.11 mM, respectively. Lineweaver-Burk analysis and molecular docking demonstrated that LLVLYYEY was a non-competitive inhibitor of alpha-glucosidase, whereas LLLLPSYSEF inhibited alpha-glucosidase, which displayed a mixed inhibition mechanism. The study suggests the possibility of using peptides from Camellia seed cake as hypoglycaemic compounds for the prevention and treatment of diabetes.
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