This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ohdan, K.
Right arrow Articles by Okada, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ohdan, K.
Right arrow Articles by Okada, S.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH
Agricola
Right arrow Articles by Ohdan, K.
Right arrow Articles by Okada, S.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, July 2000, p. 3058-3064, Vol. 66, No. 7
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Introduction of Raw Starch-Binding Domains into Bacillus subtilis alpha -Amylase by Fusion with the Starch-Binding Domain of Bacillus Cyclomaltodextrin Glucanotransferase

Kohji Ohdan,1 Takashi Kuriki,1,* Hiroki Takata,1 Hiroki Kaneko,2 and Shigetaka Okada1

Biochemical Research Laboratory, Ezaki Glico Co., Ltd., Utajima 4-6-5, Nishiyodogawa-ku, Osaka 555-8502,1 and Fundamental Research Laboratories, NEC Corporation, Miyukigaoka, Tsukuba, Ibaraki 305-0841,2 Japan

Received 25 February 2000/Accepted 18 April 2000

We constructed two types of chimeric enzymes, Ch1 Amy and Ch2 Amy. Ch1 Amy consisted of a catalytic domain of Bacillus subtilis X-23 alpha -amylase (Ba-S) and the raw starch-binding domain (domain E) of Bacillus A2-5a cyclomaltodextrin glucanotransferase (A2-5a CGT). Ch2 Amy consisted of Ba-S and D (function unknown) plus E domains of A2-5a CGT. Ch1 Amy acquired raw starch-binding and -digesting abilities which were not present in the catalytic part (Ba-S). Furthermore, the specific activity of Ch1 Amy was almost identical when enzyme activity was evaluated on a molar basis. Although Ch2 Amy exhibited even higher raw starch-binding and -digesting abilities than Ch1 Amy, the specific activity was lower than that of Ba-S. We did not detect any differences in other enzymatic characteristics (amylolytic pattern, transglycosylation ability, effects of pH, and temperature on stability and activity) among Ba-S, Ch1 Amy, and Ch2 Amy.

* Corresponding author. Mailing address: Biochemical Research Laboratory, Ezaki Glico Co., Ltd., Utajima 4-6-5, Nishiyodogawa-ku, Osaka 555-8502, Japan. Phone: 81-6-6477-8425. Fax: 81-6-6477-8362. E-mail: kuriki-takashi{at}glico.co.jp.

Applied and Environmental Microbiology, July 2000, p. 3058-3064, Vol. 66, No. 7
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Cornett, C. A.G., Fang, T.-Y., Reilly, P. J., Ford, C. (2003). Starch-binding domain shuffling in Aspergillus niger glucoamylase. Protein Eng Des Sel 16: 521-529 [Abstract] [Full Text]  
  • Kamasaka, H., Sugimoto, K., Takata, H., Nishimura, T., Kuriki, T. (2002). Bacillus stearothermophilus Neopullulanase Selective Hydrolysis of Amylose to Maltose in the Presence of Amylopectin. Appl. Environ. Microbiol. 68: 1658-1664 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»