2021
DOI: 10.1016/j.foodchem.2021.129745
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Inhibitory effect of microwave heating on cathepsin l-induced degradation of myofibrillar protein gel

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Cited by 29 publications
(10 citation statements)
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“…Ultrasound and microwave have been widely used as new physical processing methods in the protein modification of surimi gel [4] , [5] , [6] . Ultrasonic pretreatment of protein before chemical reaction can improve the effect of protein modification [4] .…”
Section: Introductionmentioning
confidence: 99%
“…Ultrasound and microwave have been widely used as new physical processing methods in the protein modification of surimi gel [4] , [5] , [6] . Ultrasonic pretreatment of protein before chemical reaction can improve the effect of protein modification [4] .…”
Section: Introductionmentioning
confidence: 99%
“…This result was similar to previous results reported by Khan et al ( 25 ) that heated and pressurized samples had lower hardness, gumminess, chewiness and higher tenderness, which was attributed to the difference between the pressure and heating medium in the exposure time. Wang et al ( 27 ) showed that compared to water bath heating, microwave heating could induce more protein cross-linking and form a denser protein gel network structure. Generally, the textural characteristics of meat treated with microwave were better.…”
Section: Resultsmentioning
confidence: 99%
“…Therefore, only few sulfhydryl groups were exposed and could form disulfide bonds at this condition. Meanwhile, at 40°C, the protein structure was destroyed by endogenous proteases, resulting in the formation of numerous disulfide bonds due to the exposure of internal sulfhydryl groups ( 36 , 37 ).…”
Section: Resultsmentioning
confidence: 99%
“…Such a decrease may also be related to endogenous proteases that acted on AC and leaded to enzymolysis. Indeed, studies showed that the cathepsin L enzyme isolated from the muscle of mature chum salmon played an active role in the hydrolysis of major protein components of myofibril, such as connectin, nebulin, myosin, a-actinin, and troponins ( 36 , 41 ). In short, the gel softening phenomenon induced by high setting temperatures resulted in the destruction of MHC and AC, which made the bands shallower and wider.…”
Section: Resultsmentioning
confidence: 99%