Digestive stability and transport ability changes of β-lactoglobulin–catechin complexes by M cell model in vitro

Yan Dai; Yan Dai; Ruoting Yang; Ruoting Yang; Yuting Yan; Yuting Yan; Yong Wu; Yong Wu; Yong Wu; Xuanyi Meng; Xuanyi Meng; Xuanyi Meng; Anshu Yang; Anshu Yang; Anshu Yang; Zhihua Wu; Zhihua Wu; Zhihua Wu; Linbo Shi; Xin Li; Xin Li; Xin Li; Hongbing Chen; Hongbing Chen; Hongbing Chen

doi:10.3389/fnut.2022.955135

Frontiers in Nutrition (Aug 2022)

Digestive stability and transport ability changes of β-lactoglobulin–catechin complexes by M cell model in vitro

Yan Dai,
Yan Dai,
Ruoting Yang,
Ruoting Yang,
Yuting Yan,
Yuting Yan,
Yong Wu,
Yong Wu,
Yong Wu,
Xuanyi Meng,
Xuanyi Meng,
Xuanyi Meng,
Anshu Yang,
Anshu Yang,
Anshu Yang,
Zhihua Wu,
Zhihua Wu,
Zhihua Wu,
Linbo Shi,
Xin Li,
Xin Li,
Xin Li,
Hongbing Chen,
Hongbing Chen,
Hongbing Chen

Affiliations

Yan Dai: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, China
Yan Dai: School of Food Science and Technology, Nanchang University, Nanchang, China
Ruoting Yang: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, China
Ruoting Yang: School of Food Science and Technology, Nanchang University, Nanchang, China
Yuting Yan: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, China
Yuting Yan: School of Food Science and Technology, Nanchang University, Nanchang, China
Yong Wu: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, China
Yong Wu: Sino-German Joint Research Institute, Nanchang University, Nanchang, China
Yong Wu: Jiangxi Province Key Laboratory of Food Allergy, Nanchang University, Nanchang, China
Xuanyi Meng: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, China
Xuanyi Meng: Sino-German Joint Research Institute, Nanchang University, Nanchang, China
Xuanyi Meng: Jiangxi Province Key Laboratory of Food Allergy, Nanchang University, Nanchang, China
Anshu Yang: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, China
Anshu Yang: Sino-German Joint Research Institute, Nanchang University, Nanchang, China
Anshu Yang: Jiangxi Province Key Laboratory of Food Allergy, Nanchang University, Nanchang, China
Zhihua Wu: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, China
Zhihua Wu: Sino-German Joint Research Institute, Nanchang University, Nanchang, China
Zhihua Wu: Jiangxi Province Key Laboratory of Food Allergy, Nanchang University, Nanchang, China
Linbo Shi: Department of Pathogen Biology and Immunology, School of Basic Medical Sciences, Nanchang University, Nanchang, China
Xin Li: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, China
Xin Li: School of Food Science and Technology, Nanchang University, Nanchang, China
Xin Li: Jiangxi Province Key Laboratory of Food Allergy, Nanchang University, Nanchang, China
Hongbing Chen: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, China
Hongbing Chen: Sino-German Joint Research Institute, Nanchang University, Nanchang, China
Hongbing Chen: Jiangxi Province Key Laboratory of Food Allergy, Nanchang University, Nanchang, China

DOI: https://doi.org/10.3389/fnut.2022.955135
Journal volume & issue: Vol. 9

Abstract

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The current research on interaction between catechin and protein has focused on non-covalent crosslinking, however, the mechanism of free radical-induced crosslinking between catechin and β-lactoglobulin (BLG) is not known. In this study, BLG bound to four catechins [epicatechin (EC), epigallocatechin (EGC), epicatechin gallate (ECG), and epigallocatechin gallate (EGCG)]. The structure change of complex was investigated by circular dichroism spectroscopy, ultraviolet-visible (UV-vis) spectroscopy and Acid and 8-Anilino-1-naphthalenesulfonic acid (ANS) fluorescence spectroscopy. M cell model was constructed to evaluate the transintestinal epithelial transport capacity of complex digestive products. The results showed that catechins were covalently bound to BLG by C-S and C-N bonds and their binding content was EGCG>EGC>ECG>EC. Moreover, catechins could change the secondary structure of BLG, with the decrease of α-helix and reduction of the irregular coilings, which leads to the loose spatial structure of the protein. Moreover, the catechin could enhance further the digestibility of BLG. Transport capacity of digestive products of M cell model was about twice of that of the Caco-2 cell model, indicating that M cell model had better antigen transport capacity. The difference between groups indicated that the transport efficiency of digestive products was decreased with the presence of catechin, in which BLG-EGCG and BLG-EGC groups were transported more strong than those of BLG-EC and BLG-ECG groups. The transport efficiency of BLG-catechin complexes were lower than that of BLG, indicating that catechin had the protective and repair roles on intestinal barrier permeability.

Published in Frontiers in Nutrition

ISSN: 2296-861X (Online)
Publisher: Frontiers Media S.A.
Country of publisher: Switzerland
LCC subjects: Technology: Home economics: Nutrition. Foods and food supply
Website: https://www.frontiersin.org/journals/nutrition/

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