作　　者： ; ; ; ;

机构地区： 华南理工大学生物科学与工程学院

出　　处： 《现代食品科技》 2009年第4期366-368,共3页

摘　　要： 以自制S-烷基-L-半胱氨酸为配基的亲和凝胶直接从独头蒜粉碎液中提取蒜氨酸酶。用自制亲和凝胶吸附蒜氨酸酶后,考察含0.2mol·L-1葡萄糖溶液的洗脱效果。利用SDS-PAGE对酶纯度进行检验,并研究温度、pH和底物浓度对酶活性的影响。结果表明,利用葡萄糖溶液洗脱,得到8.29倍的纯酶。而阴性对照纯化倍数为3.78倍。提纯的蒜氨酸酶为电泳纯,亚基约为50kDa和44kDa。以合成的蒜氨酸为底物,蒜氨酸酶的最适温度是40℃,最适pH4.92,Km为19.795μmol·mL-1,Vmax=8.446μmol·mg-1·min-1。 A method for purification of Allinase with bio-specific affmity-gel from garlic-bulb was developed. Allinase was adsorbed to affinity-gel and eluted by 0.2 mol.Ll Glucose solution. Then SDS-PAGE analysis showed that the purity of the enzyme was3.78 time higher than that without elution. Two single bands of the enzyme were found with their apparent molecular weights being of 50kDa and 44kDa, respectively. The effects of temperature, pH and subtract concentration on the enzyme activity were also studied. The most suitable temperature, pH, Km, and Vmax were 40℃, 4.92, 19.795mmol·L^-1, and 8.446μmol·mg^-1·min^-1, respectively.

关 键 词： 蒜氨酸酶 分离纯化 亲和层析

领　　域： [生物学]