TY - JOUR
T1 - Controlled Cross-Linking with Glucose Oxidase for the Enhancement of Gelling Potential of Pork Myofibrillar Protein
AU - Wang, Xu
AU - Xiong, Youling L.
AU - Sato, Hiroaki
AU - Kumazawa, Yoshiyuki
N1 - Publisher Copyright:
© 2016 American Chemical Society.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2016/12/21
Y1 - 2016/12/21
N2 - Differential oxidative modifications of myofibrillar protein (MP) by hydroxyl radicals generated in an enzymatic system with glucose oxidase (GluOx) in the presence of glucose/FeSO4 versus a Fenton system (H2O2/FeSO4) were investigated. Pork MP was modified at 4 °C and pH 6.25 with hydroxyl radicals produced from 1 mg/mL glucose in the presence of 80, 160, or 320 μg/mL GluOx and 10 μM FeSO4. Total sulfhydryl content, solubility, cross-linking pattern, and gelation properties of MP were measured. H2O2 production proceeded linearly with the concentration of GluOx and increased with reaction time. GluOx- and H2O2-dose-dependent protein polymerization, evidenced by faded myosin heavy chain and actin in SDS-PAGE as well as significant decreases in sulfhydryls, coincided with protein solubility loss. Firmer and more elastic MP gels were produced by GluOx than by the Fenton system at comparable H2O2 levels due to an altered radical reaction pathway.
AB - Differential oxidative modifications of myofibrillar protein (MP) by hydroxyl radicals generated in an enzymatic system with glucose oxidase (GluOx) in the presence of glucose/FeSO4 versus a Fenton system (H2O2/FeSO4) were investigated. Pork MP was modified at 4 °C and pH 6.25 with hydroxyl radicals produced from 1 mg/mL glucose in the presence of 80, 160, or 320 μg/mL GluOx and 10 μM FeSO4. Total sulfhydryl content, solubility, cross-linking pattern, and gelation properties of MP were measured. H2O2 production proceeded linearly with the concentration of GluOx and increased with reaction time. GluOx- and H2O2-dose-dependent protein polymerization, evidenced by faded myosin heavy chain and actin in SDS-PAGE as well as significant decreases in sulfhydryls, coincided with protein solubility loss. Firmer and more elastic MP gels were produced by GluOx than by the Fenton system at comparable H2O2 levels due to an altered radical reaction pathway.
KW - gelation
KW - glucose oxidase
KW - meat
KW - myofibrillar protein
KW - oxidation
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U2 - 10.1021/acs.jafc.6b03934
DO - 10.1021/acs.jafc.6b03934
M3 - Article
C2 - 27936702
AN - SCOPUS:85017508921
SN - 0021-8561
VL - 64
SP - 9523
EP - 9531
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 50
ER -