2021
DOI: 10.1007/s11694-021-01123-1
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Effect of oxidation modification induced by peroxyl radicals on the physicochemical and gel characteristics of grass carp myofibrillar protein

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Cited by 6 publications
(3 citation statements)
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“…Endogenous fluorescence can be used to evaluate the effect of an oxidant on the Trp residue of HDL. Free radicals can transform Trp residues with low single-electron oxidation potential into an unstable state (such as hydroperoxide and alcohol), thereby decreasing the endogenous fluorescence intensity [ 47 , 48 ]. As shown in Figure 4 A, with increasing AAPH concentration, the endogenous fluorescence intensity of HDL decreased significantly, indicating that Trp residues in HDL were converted into other products by peroxyl radicals.…”
Section: Resultsmentioning
confidence: 99%
“…Endogenous fluorescence can be used to evaluate the effect of an oxidant on the Trp residue of HDL. Free radicals can transform Trp residues with low single-electron oxidation potential into an unstable state (such as hydroperoxide and alcohol), thereby decreasing the endogenous fluorescence intensity [ 47 , 48 ]. As shown in Figure 4 A, with increasing AAPH concentration, the endogenous fluorescence intensity of HDL decreased significantly, indicating that Trp residues in HDL were converted into other products by peroxyl radicals.…”
Section: Resultsmentioning
confidence: 99%
“…ROO • can abstract hydrogen atoms from protein, leading to protein chain oxidation reactions [12]. Studies have reported that the ROO • -induced oxidation significantly affects the conformation and function of meat and soy proteins, including taste and texture [13,14]. In general, current research primarily focus on ROO • -induced protein oxidation in meat, with limited investigation of plant proteins.…”
Section: Introductionmentioning
confidence: 99%
“…At increasing hydroxyl radical concentrations, the carbonyl value and surface hydrophobicity of myofibrillar proteins typically exhibit increasing trends, and the free thiol content in myofibrillar proteins shows a decreasing trend, indicating an increased degree of protein oxidation. Gel hardness, chewiness, and elastic modulus are significantly negatively correlated with the concentration of hydroxyl radicals ( 6 ). Recently, Bao et al ( 7 ) reported that oxidation of porcine myofibrils leads to the loss of free sulfhydryl groups and histidine residues and the formation of myofibrillar protein carbonyl groups, eventually leading to the formation of large cross-linked fractions.…”
Section: Introductionmentioning
confidence: 99%