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

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 sa...

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Published inFood Chemistry: X Vol. 22; p. 101352
Main Authors Xu, Zhe, Han, Shiying, Cui, Na, Liu, Hanxiong, Yan, Xu, Chen, Hongrui, Wu, Jianping, Tan, Zhijian, Du, Ming, Li, Tingting
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier Ltd 30.06.2024
Elsevier
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Summary: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. A calcium-binding peptide from salmon targeted inhibition of amylase in digestion. [Display omitted] •Peptide IEELEELEAER(PIE) should target the inhibition of α-amylase activity.•The site of calcium binding action of PIE in α-amylase by Discovery Studio.•PIE should inhibit the differentiation of 3 T3-L1 and control body weight of mice.
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ISSN:2590-1575
2590-1575
DOI:10.1016/j.fochx.2024.101352