Anomerization and hydrolysis of lactose by beta-galactosidase from Saccharomyces lactis.
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.
Mbuyi-Kalala
A
A
Service de Chimie Générale 1 (CP160), Université Libre de Bruxelles, Belgium.
Perraudin
J P
JP
Prieels
J P
JP
D005696:Galactosidases / Q000378:metabolism*; D006868:Hydrolysis; D007536:Isomerism; D007700:Kinetics; D007785:Lactose / Q000378:metabolism*; D008962:Models, Theoretical; D012440:Saccharomyces / Q000201:enzymology*; D001616:beta-Galactosidase / Q000378:metabolism*
D005696:Galactosidases; D001616:beta-Galactosidase; D007785:Lactose