TY  - JOUR
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
PY  - 2012
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2157
AB  - 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 a-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.
PB  - Wiley, Hoboken
T2  - Biotechnology Progress
T1  - Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis
EP  - 1456
IS  - 6
SP  - 1450
VL  - 28
DO  - 10.1002/btpr.1628
ER  - 

@article{
author = "Dimitrijević, Aleksandra and Veličković, Dušan and Milosavić, Nenad and Bezbradica, Dejan",
year = "2012",
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 a-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.",
publisher = "Wiley, Hoboken",
journal = "Biotechnology Progress",
title = "Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis",
pages = "1456-1450",
number = "6",
volume = "28",
doi = "10.1002/btpr.1628"
}

Dimitrijević, A., Veličković, D., Milosavić, N.,& Bezbradica, D.. (2012). Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis. in Biotechnology Progress
Wiley, Hoboken., 28(6), 1450-1456.
https://doi.org/10.1002/btpr.1628

Dimitrijević A, Veličković D, Milosavić N, Bezbradica D. Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis. in Biotechnology Progress. 2012;28(6):1450-1456.
doi:10.1002/btpr.1628 .

Dimitrijević, Aleksandra, Veličković, Dušan, Milosavić, Nenad, Bezbradica, Dejan, "Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis" in Biotechnology Progress, 28, no. 6 (2012):1450-1456,
https://doi.org/10.1002/btpr.1628 . .