PURIFICATION AND CHARACTERIZATION OF BETA-N-ACETYLGLUCOSAMINIDASE FROM ALTEROMONAS SP STRAIN O-7

Authors
TSUJIBO H FUJIMOTO K KIMURA Y MIYAMOTO K IMADA C OKAMI Y INAMORI Y
Citation
H. Tsujibo et al., PURIFICATION AND CHARACTERIZATION OF BETA-N-ACETYLGLUCOSAMINIDASE FROM ALTEROMONAS SP STRAIN O-7, Bioscience, biotechnology, and biochemistry, 59(6), 1995, pp. 1135-1136
Citations number
10
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
Journal title
Bioscience, biotechnology, and biochemistry → ACNP
ISSN journal
09168451
Volume
59
Issue
6
Year of publication
1995
Pages
1135 - 1136
Database
ISI
SICI code
0916-8451(1995)59:6<1135:PACOBF>2.0.ZU;2-6
Abstract
beta-N-Acetylglucosaminidase (EC 3.2.1.30) was purified from the outer membrane of a marine bacterium, Alteromonas sp. strain O-7. The enzym e (GlcNAcase A) was purified by successive column chromatographies. Th e purified enzyme was found to be homogeneous on sodium dodecyl sulfat e polyacrylamide gel electrophoresis. The molecular mass and pI of Glc NAcase A were 92 kDa and 4.9, respectively. The optimum pH and tempera ture were 6.0-7.0 and 45 degrees C, respectively. GlcNAcase A was stab le up to 40 degrees C at pH 7.0, and hydrolyzed N-acetylchitooligosacc harides from dimer to hexamer. The amino-terminal 16 amino acid residu es of GlcNAcase A were sequenced.