Purification and characterization of 6-phospho-beta-galactosidase from Lactobacillus gasseri JCM 1031.
6-Phospho-beta-galactosidase from Lactobacillus gasseri JCM 1031 was purified from lactobacilli to homogeneity, about 118-fold, with 0.5% recovery by several chromatographies. The molecular mass and isoelectric point of the purified enzyme were 58 kDa and pI 5.5, respectively. The Km and Vmax for o-nitrophenyl-beta-D-galactopyranoside-6-phosphate were 0.8 mM and 116.4 mumol/min/mg, respectively. Reducing agent, Fe2+ ion, and EDTA activated but PCMB, Zn2+, and Hg2+ ions strongly inhibited the enzymatic activity.
Suzuki
M
M
Department of Applied Bio-Sciences, Tohoku University, Sendai, Japan.
Saito
T
T
Itoh
T
T
D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases; D007501:Iron / Q000737:chemistry; D007525:Isoelectric Focusing; D007778:Lactobacillus / Q000201:enzymology*; D008628:Mercury / Q000737:chemistry; D008970:Molecular Weight; D010084:Oxidation-Reduction; D015032:Zinc / Q000737:chemistry; D001616:beta-Galactosidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D007501:Iron; D006026:Glycoside Hydrolases; D001616:beta-Galactosidase; C022361:6-phospho-beta-galactosidase; D008628:Mercury; D015032:Zinc