CAJ | 학술논문

乳蛋白的氧化会使其蛋白质品质发生劣变．为了研究乳蛋白氧化聚集行为与其性质的关系，采用铁/过氧化氢/抗坏血酸(Fe/H2O2/Asc)羟自由基氧化系统诱导浓缩乳蛋白(MPC80)和酪蛋白氧化，对其聚集行为和持水性进行了分析和比较．实验证明，乳蛋白氧化聚集体分为大粒度(约1,000,nm)和小粒度(约100,nm)两个部分，氧化会使小粒度部分发生聚合，同时大粒度部分发生断裂．随着氧化值增加，MPC80和酪蛋白的持水力分别提高了0.43倍和1.73倍，酪蛋白的持水力整体高于 MPC80．以上结果表明，氧化改变了乳蛋白的聚集行为，影响其凝胶网络，在宏观上改变了乳蛋白的持水性．
유단백적양화회사기단백질품질발생렬변．위료연구유단백양화취집행위여기성질적관계，채용철/과양화경/항배혈산(Fe/H2O2/Asc)간자유기양화계통유도농축유단백(MPC80)화락단백양화，대기취집행위화지수성진행료분석화비교．실험증명，유단백양화취집체분위대립도(약1,000,nm)화소립도(약100,nm)량개부분，양화회사소립도부분발생취합，동시대립도부분발생단렬．수착양화치증가，MPC80화락단백적지수력분별제고료0.43배화1.73배，락단백적지수력정체고우 MPC80．이상결과표명，양화개변료유단백적취집행위，영향기응효망락，재굉관상개변료유단백적지수성．
Protein oxidation will result in the quality deterioration of milk protein. The changes in aggregation behavior and water binding capacity of milk protein concentrate(MPC80)and casein oxidated in a Fe/H2O2/Asc hydroxyl free radical gen-eration system(HRGS)were investigated. The results showed that the oxidated aggregation of milk protein fell into two parts:the big particle size(1,000 nm) group and the small particle size(100 nm) group. The aggregation of the latter and the fracture of the former occurred simultaneously. The waterbinding capacity of casein was greater than that of MPC80,which increased by 0.43 and 1.73 times respectively with the increase of oxidation. Thus,HRGS-mediated oxidation altered the aggregation of milk protein,which may lead to modifications of protein functionalities.