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Biocatalysts and Bioreactor Design
Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis
Article first published online: 18 OCT 2012
DOI: 10.1002/btpr.1628
Copyright © 2012 American Institute of Chemical Engineers (AIChE)
Additional Information
How to Cite
Dimitrijević, A., Veličković, D., Milosavić, N. and Bezbradica, D. (2012), Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis. Biotechnol Progress, 28: 1450–1456. doi: 10.1002/btpr.1628
Publication History
- Issue published online: 4 DEC 2012
- Article first published online: 18 OCT 2012
- Accepted manuscript online: 27 AUG 2012 11:35PM EST
- Manuscript Revised: 21 AUG 2012
- Manuscript Received: 23 FEB 2012
Funded by
- Ministry of Science of the Republic of Serbia. Grant Numbers: 172049, 046010, 451-03-00605/2012-16/51
- Abstract
- Article
- References
- Cited By
Keywords:
- transglucosylation kinetic;
- maltase;
- vanillyl alcohol;
- substrate inhibition;
- vanillyl alcohol isomaltoside
Abstract
Vanillyl alcohol glucoside is very attractive molecule due to its very powerful physiological activity. In this article, a detailed kinetic study of transglucosylation of vanillyl alcohol was performed. It was demonstrated that this reaction is very efficient (selectivity factor is 149) and occurred by a ping-pong mechanism with inhibition by glucose acceptor. At low concentration of vanillyl alcohol one additional transglucosylation product was detected. Its structure was determined to be α-isomaltoside of vanillyl alcohol, indicating that vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second, so the whole reaction mechanism was proposed. It was demonstrated that the rate of isomaltoside synthesis is two orders of magnitude smaller than glucoside synthesis, and that maltase has interestingly high Km value to maltose when vanillyl alcohol glucoside is second transglucosylation substrate. © 2012 American Institute of Chemical Engineers Biotechnol. Prog., 2012