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 Wada, K.
Right arrow Articles by Asano, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wada, K.
Right arrow Articles by Asano, Y.
Agricola
Right arrow Articles by Wada, K.
Right arrow Articles by Asano, Y.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, December 2003, p. 7058-7062, Vol. 69, No. 12
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.12.7058-7062.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Use of Borate To Control the 5'-Position-Selective Microbial Glucosylation of Pyridoxine

Koichi Wada* and Yasuhisa Asano

Biotechnology Research Center, Toyama Prefectural University, Kosugi, Toyama 939-0398, Japan

Received 26 March 2003/ Accepted 23 September 2003

Nearly 100% 5'-position selectivity of transglucosylation from maltodextrin to pyridoxine (PN) by cells of Verticillium dahliae TPU 4900 was observed when the reaction was carried out with borate. The same effect of borate was observed not only during synthesis of pyridoxine 5'-{alpha}-D-glucoside by partially purified enzyme of this strain but also during synthesis of this compound by other microorganisms and with other enzymes ({alpha}-glucosidase and cyclomaltodextrin glucanotransferase). The effect was thought to be caused by the formation of a borate complex with 3- and 4'-position hydroxyl groups of PN. A decrease in the formation of pyridoxine 5'-{alpha}-D-glucoside was observed in the reaction with borate, but this decrease was overcome by optimizing the pH and increasing the amount of cells in the reaction mixture.


* Corresponding author. Present address: Daiichi Fine Chemical Co., Ltd., 530 Chokeiji, Takaoka, Toyama 933-8511, Japan. Phone: 81-766-26-4409. Fax: 81-766-26-4462. E-mail: k-wada{at}daiichi-fcj.co.jp.


Applied and Environmental Microbiology, December 2003, p. 7058-7062, Vol. 69, No. 12
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.12.7058-7062.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Kim, N.-H., Kim, H.-J., Kang, D.-I., Jeong, K.-W., Lee, J.-K., Kim, Y., Oh, D.-K. (2008). Conversion Shift of D-Fructose to D-Psicose for Enzyme-Catalyzed Epimerization by Addition of Borate. Appl. Environ. Microbiol. 74: 3008-3013 [Abstract] [Full Text]