Double-crosslinked effect of TGase and EGCG on myofibrillar proteins gel based on physicochemical properties and molecular docking

Jinling Li; Sadia Munir; Xiaoyue Yu; Tao Yin; Juan You; Ru Liu; Shanbai Xiong; Yang Hu

doi:10.1016/j.foodchem.2020.128655

Double-crosslinked effect of TGase and EGCG on myofibrillar proteins gel based on physicochemical properties and molecular docking

Food Chem. 2021 May 30:345:128655. doi: 10.1016/j.foodchem.2020.128655. Epub 2020 Nov 19.

Authors

Jinling Li¹, Sadia Munir¹, Xiaoyue Yu¹, Tao Yin¹, Juan You¹, Ru Liu¹, Shanbai Xiong¹, Yang Hu²

Affiliations

¹ College of Food Science and Technology and MOE Key Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan 430070, PR China; Engineering Research Center of Green Development for Conventional Aquatic Biological Industry in the Yangtze River Economic Belt, Ministry of Education, Wuhan 430070, PR China.
² College of Food Science and Technology and MOE Key Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan 430070, PR China; Engineering Research Center of Green Development for Conventional Aquatic Biological Industry in the Yangtze River Economic Belt, Ministry of Education, Wuhan 430070, PR China. Electronic address: huyang@mail.hzau.edu.cn.

PMID: 33302098
DOI: 10.1016/j.foodchem.2020.128655

Abstract

The aim of this study was to determine the influence and mechanism of combining EGCG with TGase on properties of myofibrillar protein (MP) gel. A double-crosslinked effect was observed when EGCG and TGase were added into MP gel. Breaking force, deformation, water holding capacity and hardness of double-crosslinked MP gel increased by 25.3 ± 3.0 g, 0.5 ± 0.3 mm, 1.76 ± 0.4% and 34.11 ± 2.56 g, compared with those of TGase induced gel. Light microscopy and low-field nuclear magnetic resonance results indicated with EGCG content increasing, pores and structure of double-crosslinked gels became smaller and denser, T₂₂ decreased from 266.162 ms to 252.845 ms and its proportion increased from 94.103% to 96.956%. Molecular docking illustrated covalent and non-covalent interactions between EGCG and myosin heavy chain Ⅱ A, and confirmed TGase catalytic mechanism with myosin heavy chain Ⅱ A as substrate. Therefore the mixture of EGCG and TGase could be used as novel cross-linker in surimi.

Keywords: Double-crosslinking; EGCG; Molecular docking; Myofibrillar proteins; TGase.

MeSH terms

Animals
Biocatalysis*
Catechin / analogs & derivatives*
Catechin / chemistry
Chemical Phenomena*
Gels
Molecular Docking Simulation*
Muscle Proteins / chemistry*
Muscle Proteins / metabolism
Transglutaminases / metabolism*

Substances

Gels
Muscle Proteins
Catechin
epigallocatechin gallate
Transglutaminases