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 in | Food Chemistry: X Vol. 22; p. 101352 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier Ltd
30.06.2024
Elsevier |
Subjects | |
Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2590-1575 2590-1575 |
DOI: | 10.1016/j.fochx.2024.101352 |