豆粕酶解过程中蛋白质分子亚基组成及其抗原性变化

Changes in Molecular Subunit Composition and Allergenicity of Soybean Proteins during Enzymatic Hydrolysis

采用碱性蛋白酶、胰蛋白酶和木瓜蛋白酶分别水解脱脂豆粕,用SDS-PAGE分别测定水溶性酶解物和水不溶性酶解残余物中的大豆蛋白分子亚基组成,用双抗体夹心酶联免疫反应(ELISA)分别测定其抗原活性。结果表明:碱性蛋白酶和木瓜蛋白酶水解10min时,大豆7S的α’、α、β亚基和11S的酸性多肽链已基本消失,具有抗原活性的蛋白含量分别由195.90mg/g豆粕降解为90.50mg/g豆粕(碱性蛋白酶)或94.30mg/g豆粕(木瓜蛋白酶)。酶解120min时,两种酶的抗原活性去除率分别为75.70%和61.40%,而胰蛋白酶对大豆蛋白亚基和抗原性的降解效果相对较弱。

This study was to investigate the effects of enzymatic hydrolysis by three enzymes（alcalase,papain and trypsin） on molecular subunit composition and allergenicity of soybean meal proteins.The molecular subunits of soybean proteins in soluble hydrolysate and insoluble residue were analyzed with SDS-PAGE.The contents of allergenic proteins in the two hydrolysates were measured by enzyme-linked immunosorbent assay（ELISA）.The results showed that the major α’,α,β-subunits of β-conglycinin（7S） and the acidic polypeptide of glycinin（11S） in the two hydrolysates almost disappeared after hydrolysis for 10 min by alcalase or papain.The content of allergenic proteins was reduced from 195.90 mg/g soybean meal to 90.50 mg/g（alcalase） and 94.30 mg/g（papain） total hydrolysates,respectively,over half of allergenicity in soybean meal being eliminated.After 120 min hydrolysis by alcalase and papain,the rate of eliminated allergenicity was 75.70% and 61.40% respectively.Nevertheless the effect of trypsin on the molecular subunits composition and allergenic proteins was not evident compared to alcalase and papain.The results above indicated that enzymatic hydrolysis by alcalase or papain could efficiently reduce the allergenicity of soybean meal.