β-半乳糖苷酶的糖苷键作用特异性研究  

A study on the glycosidic bonds specificity of β-galactosidase from different enzyme sources

作　　者：秦燕[1] 宁正祥[1] 胡新宇[1] 

机构地区：[1]华南理工大学食品与生物工程学院

出　　处：《广东药学院学报》2001年第2期83-86,共4页Academic Journal of Guangdong College of Pharmacy

摘　　要：研究了不同微生物来源乳糖酶的糖苷键键型作用特异性 ,研究表明米曲霉乳糖酶的水解优先顺序是 β 1 6键 >β 1 4键 >β 1 3键 ,乳酸克鲁维酵母乳糖酶的水解顺序则是 β 1 4键 >β 1 6键 >β 1 3键。并发现实验所用的环状芽孢杆菌对 β 1 4键表现出了高度的键专一性。The aglycone moiety linkage specificity of β galactosidase from different enzymatic sources was investigated. The priority of susceptible bond was 1 6 linkage>1 4 linkage>1 3 linkage for A.oryzae. ,and 1 4 linkage>1 6 linkage>1 3 linkage for K.Lactis . B.circulans exhibited a considerable strict specificity for β 1 4 kinkages. The resulting disaccharides during lactose hydrolysis and the kinetic data provided further evidences for the results.

关 键 词：Β-半乳糖苷酶 糖苷糖 特异性 动力学参数 酶水解 

分 类 号：Q55[生物学—生物化学]