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Selenium-chelating corn oligopeptide as a potential antioxidant supplement: investigation of the protein conformational changes and identification of the antioxidant fragment composition

  • Xiu-Yuan Qin , Jiang-Tao Zhang , Guo-Ming Li , Mu-Yi Cai , Jun Lu , Rui-Zeng Gu EMAIL logo and Wen-Ying Liu EMAIL logo
Published/Copyright: April 15, 2020

Abstract

A selenium-chelating corn oligopeptide (Se-COP) with high protein and low molecular weight was prepared as a selenium supplement. We utilized infrared (IR), ultraviolet (UV), and circular dichroism (CD) spectroscopy, 1-anilinonaphthalene-8-sulfonate (ANS)-binding fluorescence spectra, and isothermal titration calorimetry (ITC) to analyze and describe Se-COP and its reactions. It was concluded that the chelation reaction was a spontaneous process driven by enthalpy and entropy, with ΔH=3.79 × 104 ± 4075 cal/mol, ΔS = 146 cal/mol, ΔG = –23356.30 ± 126.94 cal/mol, binding constant Ka = 1.18 × 104 ± 855 M–1, and binding site number n = 0.13 ± 0.0126, and described as coordination bonds forming and hydrophobic interaction, as well as protein conformational changes including secondary and tertiary hydrophobic structure. Se-COP had strong antioxidant capacity, and mass spectrometry (MS) was used to identify the antioxidant peptide fragment, which was characterized as LLPPY and quantified at 428.95 ng/mg. This study indicated that Se-COP prepared by chelation may be a Se supplement with antioxidant capacity that can be applied in functional foods or ingredients.


Corresponding authors: Rui-Zeng Gu, Beijing Engineering Research Center of Protein and Functional Peptides, China National Research Institute of Food and Fermentation Industries Co., Ltd., Beijing 100015, People's Republic of China, E-mail: ; and Wen-Ying Liu, Beijing Engineering Research Center of Protein and Functional Peptides, China National Research Institute of Food and Fermentation Industries Co., Ltd., Beijing 100015, People's Republic of China, E-mail:

Award Identifier / Grant number: No. 2016YFD0400604 to MC

Acknowledgment

Special thanks to the staff of the Center of Biomedical Analysis, Tsinghua University for technical assistance with LC/MS and the staff of GL Biochem (Shanghai) Ltd. for assistance with the synthesis of peptide fragments.

  1. Author contribution: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: This research was supported by grants from the National Key Research and Development Program of China (No. 2016YFD0400604 to MC).

  3. Employment or leadership: None declared.

  4. Honorarium: None declared.

  5. Conflict of interest statement: The authors declare no conflicts of interest regarding this article.

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Received: 2019-05-29
Accepted: 2020-02-20
Published Online: 2020-04-15

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