Purification and characterization of beta-N-acetylglucosaminidase from Alteromonas sp. strain O-7.
beta-N-Acetylglucosaminidase (EC 3.2.1.30) was purified from the outer membrane of a marine bacterium, Alteromonas sp. strain O-7. The enzyme (GlcNAcase A) was purified by successive column chromatographies. The purified enzyme was found to be homogeneous on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular mass and pI of GlcNAcase A were 92kDa and 4.9, respectively. The optimum pH and temperature were 6.0-7.0 and 45 degrees C, respectively. GlcNAcase A was stable up to 40 degrees C at pH 7.0, and hydrolyzed N-acetylchitooligosaccharides from dimer to hexamer. The amino-terminal 16 amino acid residues of GlcNAcase A were sequenced.
Tsujibo
H
H
Osaka University of Pharmaceutical Sciences, Japan.
Fujimoto
K
K
Kimura
Y
Y
Miyamoto
K
K
Imada
C
C
Okami
Y
Y
Inamori
Y
Y
D000118:Acetylglucosaminidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology*; D006868:Hydrolysis; D008670:Metals; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity; D013696:Temperature
D008670:Metals; D000118:Acetylglucosaminidase