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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Format: | Article |
Language: | English |
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Elsevier
2023-01-01
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Series: | Current Research in Food Science |
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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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format | Article |
id | doaj.art-80889e37dfad4757aef42b2790cb66fc |
institution | Directory Open Access Journal |
issn | 2665-9271 |
language | English |
last_indexed | 2024-03-09T00:25:27Z |
publishDate | 2023-01-01 |
publisher | Elsevier |
record_format | Article |
series | Current Research in Food Science |
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 |