posted on 2021-08-03, 18:36authored byXidong Jiao, Bowen Yan, Jianlian Huang, Jianxin Zhao, Hao Zhang, Wei Chen, Daming Fan
To
provide an insight into the oxidation behavior of cysteines
in myofibrillar proteins (MPs) during microwave heating (MW), a quantitative
redox proteomic analysis based on the isobaric iodoacetyl tandem mass
tag technology was applied in this study. MPs from silver carp muscles
were subjected to MW and water bath heating (WB) with the same time–temperature
profiles to eliminate the thermal differences caused by an uneven
energy input. Altogether, 422 proteins were found to be differentially
expressed after thermal treatments as compared to that with no heat
treatment. However, MW triggered a larger number of proteins and cysteine
sites for oxidation. Myosin heavy chain, myosin-binding protein C,
nebulin, α-actinin-3-like, and titin were found to be highly
susceptible to oxidation under microwave irradiation. Notably, MW
caused such modifications at cysteine site 9 in the head of myosin,
revealing the enhancement mechanism of MP gelation by excess cysteine
cross-linking during microwave processing. Furthermore, Gene Ontology
and functional enrichment analyses suggested that the two thermal
treatments resulted in some differences in ion binding, muscle cell
development, and protein-containing complex assembly. Overall, this
study is the first to report the redox proteomic changes caused by
MW and WB treatments, thus providing a further understanding of the
microwave-induced oxidative modifications of MPs.