Mbuyi-Kalala A, Perraudin J P, Prieels J P
Service de Chimie Générale 1 (CP160), Université Libre de Bruxelles, Belgium.
Arch Biochem Biophys. 1990 Mar;277(2):434-8. doi: 10.1016/0003-9861(90)90601-t.
Beta-Galactosidase from Saccharomyces lactis was found to be able to catalyze both the anomerization of alpha-lactose and the hydrolysis of beta-lactose; the rate of hydrolysis appeared to be four times higher with a 1:1 mixture of alpha and beta lactose than with a freshly prepared solution of alpha-lactose. The enzyme was also found to be unable to hydrolyze alpha-lactose. Thus, it appears that beta-galactosidase from S. lactis has its hydrolytic activity on lactose adapted only to the naturally more abundant beta-lactose.
已发现乳酸酵母中的β-半乳糖苷酶既能催化α-乳糖的异头化作用,又能催化β-乳糖的水解作用;对于α-乳糖和β-乳糖的1:1混合物,其水解速率似乎比新制备的α-乳糖溶液高四倍。还发现该酶不能水解α-乳糖。因此,乳酸酵母中的β-半乳糖苷酶似乎仅对天然含量更高的β-乳糖具有乳糖水解活性。