Specificity, inhibitory studies, and oligosaccharide formation by beta-galactosidase from psychrotrophic Bacillus subtilis KL88.
beta-Galactosidase from psychotrophic Bacillus subtilis KL88 was specific to the beta-D-glycosidic linkage normally present in lactose. The enzyme was completely inhibited by transition metal ions (Cu2+, Fe3+, Fe2+, Zn2+) and partially inhibited by high concentrations of glucose and galactose as well as Ca2+. It was activated by most of the alkaline earth metal ions (NA+, K+, Li+). Oligosaccharides were formed at the different levels of lactose concentrations reaching more than 20% for high lactose concentration (20%). Three types of oligosaccharides were formed in significant concentrations detected by HPLC analysis.
Rahim
K A
KA
Department of Food Science and Agricultural Chemistry, McGill University Ste. Anne de Bellevue, PQ, Canada.
Lee
B H
BH
D000818:Animals; D001412:Bacillus subtilis / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D004789:Enzyme Activation; D005690:Galactose / Q000494:pharmacology; D005947:Glucose / Q000494:pharmacology; D006868:Hydrolysis; D007785:Lactose / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology; D008673:Metals, Alkaline Earth / Q000494:pharmacology; D009844:Oligosaccharides / Q000378:metabolism*; D013379:Substrate Specificity; D001616:beta-Galactosidase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D008670:Metals; D008673:Metals, Alkaline Earth; D009844:Oligosaccharides; D001616:beta-Galactosidase; D005947:Glucose; D007785:Lactose; D005690:Galactose