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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.