Purification and characterization of alpha-L-rhamnosidase from Bacteroides JY-6, a human intestinal bacterium.
An alpha-L-rhamnosidase (EC 3.2.1.40) was purified 1500-fold from Bacteroides JY-6, an intestinal anaerobic bacterium of human. The specific activity of purified enzyme was 89.9 mumol/min/mg protein. The enzyme (M.W. 240000) is composed of two subunits of M.W. 120000 with pI and optimal pH values of 4.2 and 7.0, respectively. The apparent Kms for naringin, rutin and p-nitrophenyl-alpha-L-rhamnopyranoside were determined to be 0.89, 1.44 and 0.29 mM, respectively. The enzyme was strongly inhibited by L-rhamnose, L-fucose, saccharic acid 1,4-lactone, p-chlormercuriphenylsulfonic acid and Pb2+.
Jang
I S
IS
College of Pharmacy, Kyung-Hee University, Seoul, Korea.
Kim
D H
DH
D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification; D001439:Bacteroides / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D006801:Humans; D007422:Intestines / Q000382:microbiology*; D007700:Kinetics; D008670:Metals / Q000378:metabolism; D008970:Molecular Weight; D012210:Rhamnose / Q000378:metabolism; D013379:Substrate Specificity
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D008670:Metals; D006026:Glycoside Hydrolases; C022525:alpha-L-rhamnosidase; D012210:Rhamnose