Abstract
An α-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 μmol/min/mg protein. The enzyme (M.W. 240000) is composed of two subunits of M.W. 120000 with pl and optimal pH values of 4.2 and 7.0, respectively. The apparent K(m), for naringin, rutin and p-nitrophenyl-α-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+.
Original language | English |
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Pages (from-to) | 1546-1549 |
Number of pages | 4 |
Journal | Biological and Pharmaceutical Bulletin |
Volume | 19 |
Issue number | 12 |
DOIs | |
State | Published - Dec 1996 |
Keywords
- Bacteroides JY-6
- intestinal bacteria
- purification
- α-rhamnosidase