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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.
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'-
-D-glucoside by
partially purified enzyme of this strain but also during synthesis of
this compound by other microorganisms and with other enzymes
(
-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'-
-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.
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