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

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

doi:10.1016/j.fochx.2024.101352

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

Food Chem X. 2024 Apr 3:22:101352. doi: 10.1016/j.fochx.2024.101352. eCollection 2024 Jun 30.

Authors

Zhe Xu^{1

2

3}, Shiying Han¹, Na Cui⁴, Hanxiong Liu⁵, Xu Yan¹, Hongrui Chen⁶, Jianping Wu³, Zhijian Tan², Ming Du⁵, Tingting Li¹

Affiliations

¹ College of Life Sciences, Key Laboratory of Biotechnology and Bioresources Utilization, Dalian Minzu University, Ministry of Education, Dalian 116600, China.
² Institute of Bast Fiber Crops & Center of Southern Economic Crops, Chinese Academy of Agricultural Sciences, Changsha 410205, China.
³ Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta T6G2P5, Canada.
⁴ Department of Food and Chemical Engineering, Liuzhou Institute of Technology, Liuzhou, Guangxi 545616, China.
⁵ School of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, China.
⁶ School of Food and Bioengineering, Food Microbiology Key Laboratory of Sichuan Province, Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, Xihua University, Chengdu, Sichuan 611130, China.

Abstract

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.

Keywords: Calcium-binding; Peptide; Salmon bone; Targeted inhibition; α-amylase.