Novel strategy to improve the bioactivity and anti-hydrolysis ability of oat peptides via zinc ion-induced assembling

Junping Zhang; Yingxue Tang; Saiping Zhou; Xiaoyu Yin; Xueying Zhuang; Yanan Ren; Xiangning Chen; Junfeng Fan; Yanyan Zhang

doi:10.1016/j.foodchem.2023.135468

Novel strategy to improve the bioactivity and anti-hydrolysis ability of oat peptides via zinc ion-induced assembling

Food Chem. 2023 Aug 1:416:135468. doi: 10.1016/j.foodchem.2023.135468. Epub 2023 Jan 11.

Authors

Junping Zhang¹, Yingxue Tang¹, Saiping Zhou¹, Xiaoyu Yin¹, Xueying Zhuang¹, Yanan Ren¹, Xiangning Chen², Junfeng Fan³, Yanyan Zhang⁴

Affiliations

¹ College of Biological Sciences and Technology, Beijing Key Laboratory of Food Processing and Safety in Forestry, Beijing Forestry University, Beijing 100083, China.
² Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China; Key Laboratory of Agricultural Product Processing and Quality Control of Ministry of Agriculture and Rural Affairs, Beijing University of Agriculture, Beijing 102206, China.
³ College of Biological Sciences and Technology, Beijing Key Laboratory of Food Processing and Safety in Forestry, Beijing Forestry University, Beijing 100083, China. Electronic address: fanjunfeng@bjfu.edu.cn.
⁴ Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China. Electronic address: zhangyanyan@bac.edu.cn.

PMID: 36931140
DOI: 10.1016/j.foodchem.2023.135468

Abstract

This study aims to use metal ion coordinating method to improve the bioactivity and anti-hydrolysis ability of bioactive peptides. We demonstrated that zinc (Zn) coordination (10:1 mass ratio of peptide to Zn, pH 6.8, 37 °C) induced assembly of oat peptides, improved pancreatic lipase (PL) inhibitory activity by 30.4-36.8 % and anti-hydrolysis ability against intestinal proteases by 26.5-38.2 %; meanwhile, the peptide-Zn complex drastically reduced the PL affinity to the substrate. Detailed mechanism analysis showed that the high hydrophobicity (276 of fluorescent intensity) and dense eutectic structure of peptide-Zn complexes caused the hard hydrolysis of complexed peptides by proteases; in particular, the neutralized surface charges (∼-3.6 mV) of complexes imparted the peptide-Zn complex high affinity towards PL (-22.3 mV) thus robust PL inhibitory activity. These findings deepened our understanding of the interaction of peptides with metal elements and set the groundwork for the enhancement and protection of bioactive peptides.

Keywords: Bioaccessibility; Inhibition dynamics; Lipase inhibition; Peptides-Zn chelate; Protease; Self-assembling.

MeSH terms

Avena*
Metals / chemistry
Peptide Hydrolases
Peptides / chemistry
Peptides / pharmacology
Zinc* / chemistry

Substances

Zinc
Peptides
Metals
Peptide Hydrolases