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Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis
Author(s) -
Dimitrijević Aleksandra,
Veličković Dušan,
Milosavić Nenad,
Bezbradica Dejan
Publication year - 2012
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.1628
Subject(s) - chemistry , alcohol , glucoside , maltose , hydrolysis , maltase , substrate (aquarium) , stereochemistry , organic chemistry , enzyme , biology , medicine , ecology , alternative medicine , pathology
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 K m value to maltose when vanillyl alcohol glucoside is second transglucosylation substrate. © 2012 American Institute of Chemical Engineers Biotechnol. Prog., 2012