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Controlled Cross-Linking with Glucose Oxidase for the Enhancement of Gelling Potential of Pork Myofibrillar Protein

Wang, Xu, Xiong, Youling L., Sato, Hiroaki, Kumazawa, Yoshiyuki
Journal of agricultural and food chemistry 2016 v.64 no.50 pp. 9523-9531
actin, crosslinking, ferrous sulfate, gelation, gels, glucose, glucose oxidase, hydrogen peroxide, hydroxyl radicals, myosin heavy chains, pH, polyacrylamide gel electrophoresis, polymerization, pork, protein solubility, sulfhydryl groups
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.