Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibility

Thermo-reversible gel of myofibrillar protein (MP) can be made by tactics of elaborate deamidation using protein-glutaminase (PG), and this work aimed to disclose the link between thermally reversible gelation of MP and the coiled-coil (CC). Enzymatic deamidation fragmented myofibril filaments and t...

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Main Authors: Lingying Zhang, Yanna Zhang, Yue Wang, Xing Chen
Format: Article
Language:English
Published: Elsevier 2023-01-01
Series:Current Research in Food Science
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S266592712300179X
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author Lingying Zhang
Yanna Zhang
Yue Wang
Xing Chen
author_facet Lingying Zhang
Yanna Zhang
Yue Wang
Xing Chen
author_sort Lingying Zhang
collection DOAJ
description Thermo-reversible gel of myofibrillar protein (MP) can be made by tactics of elaborate deamidation using protein-glutaminase (PG), and this work aimed to disclose the link between thermally reversible gelation of MP and the coiled-coil (CC). Enzymatic deamidation fragmented myofibril filaments and triggered structural reassembly to create small-sized aggregates. The coiling and dissociation of CC structure in the myosin tails is the fundamental structural basis of the PG deamidated MP (DMP) in the dynamic evolution of reversible gelation. After specific inhibition of CC assembly by trifluoroethanol (TFE), the thermo-reversible gel ability of DMP was impaired, which confirmed that the dynamic assembly of CC with temperature response played a key role in the thermo-reversible gelation of DMP. The findings may broaden the molecular basis of natural CC reversible gelation and foster advances for the development of new muscle protein products.
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spelling doaj.art-80889e37dfad4757aef42b2790cb66fc2023-12-12T04:36:08ZengElsevierCurrent Research in Food Science2665-92712023-01-017100611Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibilityLingying Zhang0Yanna Zhang1Yue Wang2Xing Chen3State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, ChinaState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, ChinaState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, ChinaState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, China; Corresponding author. State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, China.Thermo-reversible gel of myofibrillar protein (MP) can be made by tactics of elaborate deamidation using protein-glutaminase (PG), and this work aimed to disclose the link between thermally reversible gelation of MP and the coiled-coil (CC). Enzymatic deamidation fragmented myofibril filaments and triggered structural reassembly to create small-sized aggregates. The coiling and dissociation of CC structure in the myosin tails is the fundamental structural basis of the PG deamidated MP (DMP) in the dynamic evolution of reversible gelation. After specific inhibition of CC assembly by trifluoroethanol (TFE), the thermo-reversible gel ability of DMP was impaired, which confirmed that the dynamic assembly of CC with temperature response played a key role in the thermo-reversible gelation of DMP. The findings may broaden the molecular basis of natural CC reversible gelation and foster advances for the development of new muscle protein products.http://www.sciencedirect.com/science/article/pii/S266592712300179XMyofibrillar proteinThermo-reversible gelCoiled-coilProtein glutaminaseTrifluoroethanol
spellingShingle Lingying Zhang
Yanna Zhang
Yue Wang
Xing Chen
Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibility
Current Research in Food Science
Myofibrillar protein
Thermo-reversible gel
Coiled-coil
Protein glutaminase
Trifluoroethanol
title Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibility
title_full Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibility
title_fullStr Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibility
title_full_unstemmed Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibility
title_short Thermo-reversible gelation of myofibrillar protein: Relationship between coiled-coil and thermal reversibility
title_sort thermo reversible gelation of myofibrillar protein relationship between coiled coil and thermal reversibility
topic Myofibrillar protein
Thermo-reversible gel
Coiled-coil
Protein glutaminase
Trifluoroethanol
url http://www.sciencedirect.com/science/article/pii/S266592712300179X
work_keys_str_mv AT lingyingzhang thermoreversiblegelationofmyofibrillarproteinrelationshipbetweencoiledcoilandthermalreversibility
AT yannazhang thermoreversiblegelationofmyofibrillarproteinrelationshipbetweencoiledcoilandthermalreversibility
AT yuewang thermoreversiblegelationofmyofibrillarproteinrelationshipbetweencoiledcoilandthermalreversibility
AT xingchen thermoreversiblegelationofmyofibrillarproteinrelationshipbetweencoiledcoilandthermalreversibility