Oxidative stability of isoelectric solubilization/precipitation-isolated PSE-like chicken protein.


Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Key Laboratory of Animal Products Processing, MOA, Key Lab of Meat Processing and Quality Control, MOE, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, PR China. Electronic address: [Email]


The effects of a hydroxyl radical generating system (Fe3+/H2O2) at different H2O2 concentrations (0, 1 and 10 mM) on the chemical and structural properties of isoelectric solubilization/precipitation (ISP)-isolated PSE (pale, soft, exudative)-like chicken protein were investigated. Both acid and alkaline treatments effectively reduced the pro-oxidant contents in PSE-like meat systems, such as lipids, pigments and myoglobins. The ISP samples generated less carbonyl derivatives and Schiff base but yielded higher sulfhydryl and free amine loss in response to oxidation. Correspondingly, sulfur-contained amino acids in ISP samples were more easily converted, even at the 1-mM H2O2 concentration, than in the PSE-like meat paste. Moreover, the ISP-isolated proteins have possibly maintained their gelling properties after oxidation compared to the PSE-like meat paste. In regards to chemical and structural modification, the ISP treated protein showed a different susceptibility to oxidation in vitro.


Chemical modification,Isoelectric solubilization/precipitation,PSE-like,Protein oxidation,