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

作者：Zhe Xu, Shiying Han, Na Cui, Hanxiong Liu, Yan Xu, Hongrui Chen, Jianping Wu, Zhijian Tan, Ming Du, Tingting Li · 发表于：Food Chemistry X · 年份：2024 · DOI：10.1016/j.fochx.2024.101352 · 被引用次数：5 · 研究领域：Protein Hydrolysis and Bioactive Peptides、Aquaculture Nutrition and Growth、Meat and Animal Product Quality

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.