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Applied and Environmental Microbiology, April 2002, p. 1658-1664, Vol. 68, No. 4
0099-2240/02/$04.00+0 DOI: 10.1128/AEM.68.4.1658-1664.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Biochemical Research Laboratory, Ezaki Glico Co., Ltd., Nishiyodogawa-ku, Osaka 555-8502, Japan
Received 31 October 2001/ Accepted 8 January 2002
The specificity of Bacillus stearothermophilus TRS40 neopullulanase toward amylose and amylopectin was analyzed. Although this neopullulanase completely hydrolyzed amylose to produce maltose as the main product, it scarcely hydrolyzed amylopectin. The molecular mass of amylopectin was decreased by only one order of magnitude, from approximately 108 to 107 Da. Furthermore, this neopullulanase selectively hydrolyzed amylose when starch was used as a substrate. This phenomenon, efficient hydrolysis of amylose but not amylopectin, was also observed with cyclomaltodextrinase from alkaliphilic Bacillus sp. strain A2-5a and maltogenic amylase from Bacillus licheniformis ATCC 27811. These three enzymes hydrolyzed cyclomaltodextrins and amylose much faster than pullulan. Other amylolytic enzymes, such as bacterial saccharifying
-amylase, bacterial liquefying
-amylase, ß-amylase, and neopullulanase from Bacillus megaterium, did not exhibit this distinct substrate specificity at all, i.e., the preference of amylose to amylopectin.
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