Bioscience Biotechnology and Biochemistry · 1995 · 10 citations · 0 references
Life SciencesBiochemistryMicrobiologyEnzymologyMarine MicrobiologyProtein BiochemistryEnzyme CharacterizationEnzyme PurificationGlycan AnalysisGlycan BiosynthesisGlycan DegradationMicrobial GlycobiologyBacterial Protein GlycosylationCarbohydrate-active Marine EnzymesMarine Bacterial EnzymesMarine Enzyme CharacterizationMarine Enzyme PurificationMolecular Mass DeterminationOuter Membrane ProteinsPolysaccharide Purification
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.