Preparation and identification of a novel peptide with high antioxidant activity from corn gluten meal

Xiao Yu; Yanan Chen; Zhiguo Qi; Quan Chen; Yujin Cao; Qingshan Kong

doi:10.1016/j.foodchem.2023.136389

Preparation and identification of a novel peptide with high antioxidant activity from corn gluten meal

Food Chem. 2023 Oct 30:424:136389. doi: 10.1016/j.foodchem.2023.136389. Epub 2023 May 15.

Authors

Xiao Yu¹, Yanan Chen², Zhiguo Qi², Quan Chen³, Yujin Cao⁴, Qingshan Kong²

Affiliations

¹ CAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
² CAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China.
³ CAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China. Electronic address: chenquan@qibebt.ac.cn.
⁴ CAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China. Electronic address: caoyj@qibebt.ac.cn.

PMID: 37209437
DOI: 10.1016/j.foodchem.2023.136389

Abstract

The antioxidant activity of corn peptides is related to their molecular weight and structure. Corn gluten meal (CGM) was hydrolyzed using a combination of Alcalase, Flavorzyme and Protamex, and the hydrolysates were subjected to antioxidant activity analysis after further fractionation. Corn peptides with molecular weights less than 1 kDa (CPP1) exhibited excellent antioxidant activity. A novel peptide, Arg-Tyr-Leu-Leu (RYLL), was identified from CPP1. RYLL displayed preferable scavenging capacities for ABTS radicals and DPPH radicals, with IC₅₀ values of 0.122 mg/ml and 0.180 mg/ml, respectively. Based on quantum calculations, RYLL had multiple antioxidant active sites, and tyrosine was the main active site due to the highest energy of the highest occupied molecular orbit (HOMO). Moreover, the simple peptide structure and hydrogen bond network of RYLL contributed to the exposure of the active site. This study elucidated the antioxidant mechanism of corn peptides, which could provide an understanding for CGM hydrolysates as natural antioxidants.

Keywords: Antioxidant mechanism; Corn gluten meal; Enzyme hydrolysis; Quantum calculation; Structure-activity relationship.

MeSH terms

Antioxidants* / chemistry
Glutens* / chemistry
Hydrolysis
Peptides / chemistry
Protein Hydrolysates / chemistry
Zea mays / chemistry

Substances

Antioxidants
Glutens
Peptides
Protein Hydrolysates