Identification and characterization of a calcium-binding peptide from salmon bone for the targeted inhibition of α-amylase in digestion

文献类型： 外文期刊

第一作者： Xu, Zhe

作者： Xu, Zhe;Han, Shiying;Yan, Xu;Li, Tingting;Cui, Na;Xu, Zhe;Tan, Zhijian;Xu, Zhe;Wu, Jianping;Liu, Hanxiong;Du, Ming;Chen, Hongrui

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关键词： Targeted inhibition; alpha-amylase; Calcium-binding; Salmon bone; Peptide

期刊名称：FOOD CHEMISTRY-X （ 影响因子：6.1； 五年影响因子：6.4 ）

ISSN： 2590-1575

年卷期： 2024 年 22 卷

页码：

收录情况： SCI

摘要： alpha-Amylase, essential for carbohydrate digestion, relies on calcium (Ca) for its structural integrity and enzymatic activity. This study explored the inhibitory effect of salmon bone peptides on alpha-amylase activity through their interaction with the enzyme's Ca -binding sites. Among the various salmon bone hydrolysates, salmon bone trypsin hydrolysate (SBTH) exhibited the highest alpha-amylase inhibition. The peptide IEELEEELEAER (PIE), with a sequence of Ile-Glu-Glu-Leu-Glu-Glu-Glu-Glu-Leu-Glu-Ala-Glu-Arg from SBTH, was found to specifically target the Ca -binding sites in alpha-amylase, interacting with key residues such as Asp206, Trp203, His201, etc. Additionally, cellular experiments using 3 T3 -L1 preadipocytes indicated PIE's capability to suppress adipocyte differentiation, and decreases in intracellular triglycerides, total cholesterol, and lipid accumulation. In vivo studies also showed a significant reduction in weight gain in the group treated with PIE(6.61%)compared with the control group (33.65%). These findings suggest PIE is an effective alpha-amylase inhibitor, showing promise for obesity treatment.

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