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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

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

作者机构：

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

期刊名称： Food Chemistry: X

ISSN： 2590-1575

年卷期： 2024 年 22 卷

页码：

收录情况： SCIE（2024版） ; ; EI（2024版）

摘要： α-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 α-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 α-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 α-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 α-amylase inhibitor, showing promise for obesity treatment.

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