Journal
JOURNAL OF FOOD SCIENCE
Volume 87, Issue 7, Pages 2932-2942Publisher
WILEY
DOI: 10.1111/1750-3841.16166
Keywords
mu-calpain; hydroxyl radical; myofibrillar protein; protein degradation; tan mutton
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Funding
- National Natural Science Foundation of China [31960460]
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This study investigated the oxidative modification of mutton myofibrillar protein (MP) by hydroxyl radicals (OH) and its impact on the proteolysis of MP by mu-calpain. The results showed that OH can alter the physicochemical properties of MP and its susceptibility to mu-calpain.
Tenderness affects mutton quality and price, and the degradation of myofibrillar protein (MP) is critical to improve tenderness. We investigated the oxidative modification of mutton MP by hydroxyl radicals (OH) and the effects of this modification on the proteolysis of MP by mu-calpain. As the H2O2 concentrations increased, the carbonyl and dityrosine contents and the surface hydrophobicity of MP all display an increasing trend, whereas the total sulfhydryl and intrinsic fluorescence intensity of MP declines significantly. SDS-PAGE electrophoresis indicates that disulfide bonds and other covalent bonds led to protein cross-linking and aggregation. After adding mu-calpain, with increasing oxidation, the degradation percentage of myosin heavy chain (MHC) increases considerably and actin degradation is promoted, while the proteolysis of troponin-T and desmin is inhibited. These data suggest that center dot OH can change MP physicochemical properties and its susceptibility to mu-calpain. Future investigations will focus on the effect of oxidation on the degradation of MP by other proteases, such as cathepsins and caspase and the effect of oxidation on these enzymes.
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