Enrichment of antioxidant peptides by interfacial modification of oat polypeptides induced by zinc ions

Xiaoyu Yin; Zhenchi Yang; Weihe Shi; Shuheng Fan; Xinyue Guan; Yanan Ren; Hongfei Zhao; Junfeng Fan; Mengze Wang; Jianjun Li

doi:10.1016/j.ijbiomac.2024.138573

Enrichment of antioxidant peptides by interfacial modification of oat polypeptides induced by zinc ions

Int J Biol Macromol. 2024 Dec 10:138573. doi: 10.1016/j.ijbiomac.2024.138573. Online ahead of print.

Authors

Xiaoyu Yin¹, Zhenchi Yang², Weihe Shi², Shuheng Fan³, Xinyue Guan¹, Yanan Ren¹, Hongfei Zhao¹, Junfeng Fan⁴, Mengze Wang⁵, Jianjun Li⁶

Affiliations

¹ College of Biological Sciences and Technology, Beijing Key Laboratory of Food Processing and Safety in Forestry, Beijing Forestry University, Beijing, China.
² School of Statistics, University of International Business and Economics, Beijing, China.
³ China School of Banking and Finance, University of International Business and Economics, Beijing, China.
⁴ College of Biological Sciences and Technology, Beijing Key Laboratory of Food Processing and Safety in Forestry, Beijing Forestry University, Beijing, China. Electronic address: fanjunfeng@bjfu.edu.cn.
⁵ College of Food Science and Engineering, Ningxia University, Yinchuan, China. Electronic address: wangmengze@nxu.edu.cn.
⁶ Ningxia Xianeng Biotechnology Co., Ltd, Lingwu, China.

PMID: 39667476
DOI: 10.1016/j.ijbiomac.2024.138573

Abstract

The pursuit of methods to enhance the purity of food-sourced bioactive peptides continues to pose significant challenges. This study introduces an innovative approach to enrich antioxidant peptides by using zinc ion coordination to augment the foaming capabilities of oat peptides. The resulting antioxidant peptide fraction (AF) accounted for 18 % of the oat globulin hydrolysates, with a significant increase (22-47 %) in scavenging activity against 2,2-diphenyl-1-picrylhydrazyl (DPPH), OH, and O₂^- radicals. Proteomics identified 479 peptide segments within AF, and the HipHop analysis further identified 340 antioxidant peptides. Notably, the larger peptides (7-23 amino acids) were the primary contributors to the antioxidant activity, featuring key pharmacophores, i.e., charge centers, hydrophobic centers, and hydrogen bond acceptors. The AF and its key monomers (DDTKTWPEDL, YSTDPANPTKSA, NKREQQSGNNIF, and QVGQSPQYQEG) exhibited potent inhibitory effects on tyrosinase (IC₅₀, 18.60-46.20 μg/mL) and provided strong inhibition against lipid oxidation, indicating great potential for applications in health supplements and food preservation.

Keywords: Antioxidant peptide; Foaming property; Metal coordination; Oat peptides; Pharmacophore.