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Effects of magnetic nanoscale combined radio frequency or microwave thawing on conformation of sea bass myosin heavy chain: a molecular dynamics study.

Authors :
Zhang, Wendi
Tian, Fang
Liu, Shucheng
Cai, Luyun
Source :
Journal of the Science of Food & Agriculture; Jan2023, Vol. 103 Issue 2, p856-864, 9p
Publication Year :
2023

Abstract

BACKGROUND: The consumption of frozen foods inevitably involves a thawing process. Protein conformation changes during a short thawing process and the quantification of their effects remains challenging. Molecular dynamics simulations can be used to evaluate the conformational changes of protein occurring in food processing. RESULTS: In the present study, four different thawing methods were used [i.e. magnetic nanometer combined with microwave thawing (MT‐Mag), magnetic nanometer combined with radio frequency thawing (RT‐Mag), radio frequency thawing (RT) and microwave thawing (MT)] to change the conformation of myosin heavy chain (MHC). The results obtained showed that, compared with the fresh sample, the hydrogen bond number and radius of gyration of the RT‐Mag and RT groups were less decreased. Visual molecular dynamics STRIDE analysis showed that the content of the α helix was relatively high in the RT‐Mag and MT‐Mag groups. CONCLUSION: These simulation results indicate that RT‐Mag can be used as an effective method for promoting the thawing process of fish and better stabilizing the protein structure. These conclusions provide a theoretical realization for understanding the protein conformational transition during the thawing process and the realization of quantification and also provide guidance for choosing better thawing conditions without loss of nutritional properties. © 2022 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00225142
Volume :
103
Issue :
2
Database :
Complementary Index
Journal :
Journal of the Science of Food & Agriculture
Publication Type :
Academic Journal
Accession number :
160589599
Full Text :
https://doi.org/10.1002/jsfa.12197