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Food Science of Animal Products 2023, 1(1): 9240004 https://doi.org/10.26599/FSAP.2023.9240004
Research Article | Open Access | Issue | Published: 07 March 2023

Effects of biopolymer ratio and pH value on the complex formation between whey protein isolates and soluble Auricularia auricular polysaccharides

Show Author's Information Xiuliang Li1,2,3,  Yang Su1,2,  Xiaoyun Han1,2,4,  Qixin Yan1,2,  Qingshen Sun1,2,4( )
Engineering Research Center of Agricultural Microbiology Technology, Ministry of Education, Heilongjiang University, Harbin 150500, China
Jiaxiang Research Academy of Industrial Technology, Jining 272400, China
Key Laboratory of Molecular Biology, College of Heilongjiang Province, School of Life Sciences, Heilongjiang University, Harbin 150080, China
Key Laboratory of Microbiology, College of Heilongjiang Province, School of Life Sciences, Heilongjiang University, Harbin 150080, China
Keywords:
interaction, whey protein isolate, Auricularia auricular polysaccharides, docking
Cite this article:
Li X, Su Y, Han X, et al. Effects of biopolymer ratio and pH value on the complex formation between whey protein isolates and soluble Auricularia auricular polysaccharides. Food Science of Animal Products, 2023, 1(1): 9240004. https://doi.org/10.26599/FSAP.2023.9240004
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Abstract Full text About this article

Biopolymer complexes fabricated by proteins and neutral polysaccharides have some specific and innovative functionalities. A better understanding of the interactions among these biopolymers might provide new insight into the applications of the complexes. Therefore, this study aimed to investigate the structural characteristics and molecular interaction mechanisms of whey protein isolates (WPI) and Auricularia auricular polysaccharides (APs). The turbidity analysis confirmed that the pH value and mixing ratio of the two polymers had strong effects on the formation of the APs-WPI complexes. All dispersions formed soluble complexes at approximately pH = 6.0 (pHc). APs-WPI self-assembles exhibited physically cross-linked networks under higher APs proportions, while they formed spherical complexes at higher WPI ratios. The addition of APs could alter the secondary structure of WPI, and the most noticeable changes were located in the regions of β-sheet and β-turn as confirmed by circular dichroism (CD) analysis. A molecular docking study showed that the amino acid residues of β-lactoglobulin complexed with the –COOH and –OH groups of APs. Hydrogen bonds and hydrophobic interactions, which were nonbonding contributions, played a key role in the formation of the APs-WPI complex. This study provided a basis for the development and application of APs in WPI-based beverages.


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About this article

Effects of biopolymer ratio and pH value on the complex formation between whey protein isolates and soluble Auricularia auricular polysaccharides

Show Author's information Xiuliang Li1,2,3, Yang Su1,2, Xiaoyun Han1,2,4, Qixin Yan1,2, Qingshen Sun1,2,4( )
Engineering Research Center of Agricultural Microbiology Technology, Ministry of Education, Heilongjiang University, Harbin 150500, China
Jiaxiang Research Academy of Industrial Technology, Jining 272400, China
Key Laboratory of Molecular Biology, College of Heilongjiang Province, School of Life Sciences, Heilongjiang University, Harbin 150080, China
Key Laboratory of Microbiology, College of Heilongjiang Province, School of Life Sciences, Heilongjiang University, Harbin 150080, China

Abstract

Biopolymer complexes fabricated by proteins and neutral polysaccharides have some specific and innovative functionalities. A better understanding of the interactions among these biopolymers might provide new insight into the applications of the complexes. Therefore, this study aimed to investigate the structural characteristics and molecular interaction mechanisms of whey protein isolates (WPI) and Auricularia auricular polysaccharides (APs). The turbidity analysis confirmed that the pH value and mixing ratio of the two polymers had strong effects on the formation of the APs-WPI complexes. All dispersions formed soluble complexes at approximately pH = 6.0 (pHc). APs-WPI self-assembles exhibited physically cross-linked networks under higher APs proportions, while they formed spherical complexes at higher WPI ratios. The addition of APs could alter the secondary structure of WPI, and the most noticeable changes were located in the regions of β-sheet and β-turn as confirmed by circular dichroism (CD) analysis. A molecular docking study showed that the amino acid residues of β-lactoglobulin complexed with the –COOH and –OH groups of APs. Hydrogen bonds and hydrophobic interactions, which were nonbonding contributions, played a key role in the formation of the APs-WPI complex. This study provided a basis for the development and application of APs in WPI-based beverages.

Keywords: interaction, whey protein isolate, Auricularia auricular polysaccharides, docking

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Received: 12 December 2022
Revised: 03 January 2023
Accepted: 25 January 2023
Published: 07 March 2023
Issue date: March 2023

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© Beijing Academy of Food Sciences 2023.

Acknowledgements

This study was funded by the Heilongjiang Province Natural Science Foundation of China (Nos. LH2021C075 and LH2022C075).

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Food Science of Animal Products published by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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