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Applied and Environmental Microbiology, April 2001, p. 1744-1750, Vol. 67, No. 4
Tochigi Research Laboratories of Kao
Corporation, 2606 Akabane, Ichikai, Haga, Tochigi 321-3497, Japan
Received 9 October 2000/Accepted 2 February 2001
A novel
0099-2240/01/$04.00+0 DOI: 10.1128/AEM.67.4.1744-1750.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Novel
-Amylase That Is Highly Resistant to
Chelating Reagents and Chemical Oxidants from the Alkaliphilic
Bacillus Isolate KSM-K38
-amylase (AmyK38) was found in cultures of an
alkaliphilic Bacillus isolate designated KSM-K38. Based
on the morphological and physiological characteristics and phylogenetic
position as determined by 16S ribosomal DNA gene sequencing and DNA-DNA
reassociation analysis, it was suggested that the isolate was a new
species of the genus Bacillus. The enzyme had an optimal
pH of 8.0 to 9.5 and displayed maximum catalytic activity at 55 to
60°C. The apparent molecular mass was approximately 55 kDa, as
determined by sodium dodecyl sulfate-polyacrylamide gel
electrophoresis, and the isoelectric point was around pH 4.2. This
enzyme efficiently hydrolyzed various carbohydrates to yield
maltotriose, maltohexaose, maltoheptaose, and, in addition, maltose as
major end products after completion of the reaction. The activity was
not prevented at all by EDTA and EGTA at concentrations as high as 100 mM. Moreover, AmyK38 was highly resistant to chemical oxidation and
maintained more than 80% of its original activity even after
incubation for 1 h in the presence of excess
H2O2 (1.8 M).
*
Corresponding author. Mailing address: Tochigi Research
Laboratories of Kao Corporation, 2606 Akabane, Ichikai, Haga, Tochigi 321-3497, Japan. Phone: 81 (285) 68-7516. Fax: 81 (285) 68-7547. E-mail: 400297{at}kastanet.kao.co.jp.
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