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

被引：98
作者：
Li, Jinling [1 ,2 ,3 ]
Munir, Sadia [1 ,2 ,3 ]
Yu, Xiaoyue [1 ,2 ,3 ]
Yin, Tao [1 ,2 ,3 ]
You, Juan [1 ,2 ,3 ]
Liu, Ru [1 ,2 ,3 ]
Xiong, Shanbai [1 ,2 ,3 ]
Hu, Yang [1 ,2 ,3 ]
机构：
[1] Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Peoples R China
[2] Huazhong Agr Univ, MOE Key Lab Environm Correlat Dietol, Wuhan 430070, Peoples R China
[3] Minist Educ, Engn Res Ctr Green Dev Convent Aquat Biol Ind Yan, Wuhan 430070, Peoples R China
来源：
FOOD CHEMISTRY | 2021年 / 345卷
基金：
国家重点研发计划;
关键词：
Myofibrillar proteins; TGase; EGCG; Double-crosslinking; Molecular docking;
D O I：
10.1016/j.foodchem.2020.128655
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
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, T-22 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.
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页数：10
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