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.
|Number of pages||9|
|Journal||Journal of Agricultural and Food Chemistry|
|State||Published - Dec 21 2016|
Bibliographical noteFunding Information:
This research was supported by the USDA National Institute of Food and Agriculture (Hatch Project 1005724), Ajinomoto Co., Inc., Japan, and an Oversea Study Fellowship from the China Scholarship Council (to X.W.). Approved for publication as journal article no. 16-07-040 by the Director of the Kentucky Agricultural Experiment Station.
- glucose oxidase
- myofibrillar protein
ASJC Scopus subject areas
- Chemistry (all)
- Agricultural and Biological Sciences (all)