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Updated: Nov 26, 2025

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
Published on: August 22, 2018
Double-crosslinked effect of TGase and EGCG on myofibrillar proteins gel based on physicochemical properties and
Jinling Li1, Sadia Munir1, Xiaoyue Yu1
1College 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.
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.
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