Affiliation:
1. Bacteriology Group1and
2. Microbiology Group,2 International Centre for Genetic Engineering and Biotechnology, I-34012 Trieste, Italy
Abstract
ABSTRACT
Bacillus pumilus
PS213 was found to be able to release acetate from acetylated xylan. The enzyme catalyzing this reaction has been purified to homogeneity and characterized. The enzyme was secreted, and its production was induced by corncob powder and xylan. Its molecular mass, as determined by gel filtration, is 190 kDa, while sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed a single band of 40 kDa. The isoelectric point was found to be 4.8, and the enzyme activity was optimal at 55°C and pH 8.0. The activity was inhibited by most of the metal ions, while no enhancement was observed. The Michaelis constant (
K
m
) and
V
max
for α-naphthyl acetate were 1.54 mM and 360 μmol min
−1
mg of protein
−1
, respectively.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Reference22 articles.
1. Cooperativity of esterases and xylanases in the enzymatic degradation of acetyl xylan.;Biely P.;Bio/Technology,1986
2. Acetyl xylan esterases in fungal cellulolytic systems.;Biely P.;FEBS Lett.,1985
3. Biely
P.
MacKenzie
C. R.
Schneider
H.
Puls
J.
The role of fungal acetyl xylan esterases in the degradation of acetyl xylan by fungal xylanases
Wood and cellulosics.
Kennedy
J. F.
Phillips
G. O.
Williams
P. A.
1987
283
289
Ellis Horwood Ltd.
New York N.Y
4. Esterases of xylan-degrading microorganisms: production, properties, and significance.;Christov L. P.;Enzyme Microb. Technol.,1993
5. Purification and characterization of ferulate and p-coumarate decarboxylase from Bacillus pumilus
Cited by
47 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献