LAUSR

BACKGROUND The consumption of frozen foods inevitably involves thawing process. Protein conformation changes during a short thawing process and quantifying their effects is challenging. Molecular dynamics simulations can be used to evaluate the conformational changes of protein occurring in food processing. RESULTS In this 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 obtained results 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 (VMD) 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 to promote the thawing process of fish and better stabilize the protein structure. These conclusions provide a theoretical realization of understanding the protein conformational transition during the thawing process and the realization of quantification and provide guidance to choose better thawing conditions without loss of nutritional properties. This article is protected by copyright. All rights reserved.