Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Purification and Characterization of β-N-Acetylglucosaminidase from Alteromonas sp.Strain O-7
Hiroshi TsujiboKazuhiro FujimotoYoshihisa KimuraKatsushiro MiyamotoChiaki ImadaYoshiro OkamiYoshihiko Inamori
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1995 Volume 59 Issue 6 Pages 1135-1136

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Abstract

β-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 92 kDa and 4.9, respectively. The optimum pH and temperature were 6.0-7.0and 45°C, respectively. GlcNAcase A was stable up to 40°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.

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