In this study, enzymatic synthesis of galactoside of salicin, compound with potential physiological activity due to structural resemblance with galectin inhibitors, and analgesic and antipyretic properties of salicin, was performed using beta-galactosidase from Aspergillus oryzae. It was determined, using HPLC and ion mobility mass spectrometry, that enzymatic synthesis was highly selective since only one isomer was formed via primary hydroxyl group on glucose moiety of salicin. The optimization of key experimental factors using response surface methodology enabled galactosyl salicin concentration up to 30.8 mM obtained at lactose concentration 40 mM, salicin concentration 110 mM, enzyme amount 360 IU and reaction time 12 h.
TY - JOUR
AU - Simović, Milica
AU - Veličković, Dušan
AU - Stojanović, Marija
AU - Milosavić, Nenad
AU - Rogniaux, Helene
AU - Ropartz, David
AU - Bezbradica, Dejan
PY - 2015
UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3018
AB - In this study, enzymatic synthesis of galactoside of salicin, compound with potential physiological activity due to structural resemblance with galectin inhibitors, and analgesic and antipyretic properties of salicin, was performed using beta-galactosidase from Aspergillus oryzae. It was determined, using HPLC and ion mobility mass spectrometry, that enzymatic synthesis was highly selective since only one isomer was formed via primary hydroxyl group on glucose moiety of salicin. The optimization of key experimental factors using response surface methodology enabled galactosyl salicin concentration up to 30.8 mM obtained at lactose concentration 40 mM, salicin concentration 110 mM, enzyme amount 360 IU and reaction time 12 h.
PB - Elsevier Sci Ltd, Oxford
T2 - Process Biochemistry
T1 - Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by beta-galactosidase from Aspergillus oryzae
EP - 788
IS - 5
SP - 782
VL - 50
DO - 10.1016/j.procbio.2015.01.028
ER -
@article{
author = "Simović, Milica and Veličković, Dušan and Stojanović, Marija and Milosavić, Nenad and Rogniaux, Helene and Ropartz, David and Bezbradica, Dejan",
year = "2015",
url = "http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3018",
abstract = "In this study, enzymatic synthesis of galactoside of salicin, compound with potential physiological activity due to structural resemblance with galectin inhibitors, and analgesic and antipyretic properties of salicin, was performed using beta-galactosidase from Aspergillus oryzae. It was determined, using HPLC and ion mobility mass spectrometry, that enzymatic synthesis was highly selective since only one isomer was formed via primary hydroxyl group on glucose moiety of salicin. The optimization of key experimental factors using response surface methodology enabled galactosyl salicin concentration up to 30.8 mM obtained at lactose concentration 40 mM, salicin concentration 110 mM, enzyme amount 360 IU and reaction time 12 h.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by beta-galactosidase from Aspergillus oryzae",
pages = "788-782",
number = "5",
volume = "50",
doi = "10.1016/j.procbio.2015.01.028"
}
Simović, M., Veličković, D., Stojanović, M., Milosavić, N., Rogniaux, H., Ropartz, D.,& Bezbradica, D. (2015). Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by beta-galactosidase from Aspergillus oryzae.
Process Biochemistry
Elsevier Sci Ltd, Oxford., 50(5), 782-788.
https://doi.org/10.1016/j.procbio.2015.01.028
Simović M, Veličković D, Stojanović M, Milosavić N, Rogniaux H, Ropartz D, Bezbradica D. Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by beta-galactosidase from Aspergillus oryzae. Process Biochemistry. 2015;50(5):782-788
Simović Milica, Veličković Dušan, Stojanović Marija, Milosavić Nenad, Rogniaux Helene, Ropartz David, Bezbradica Dejan, "Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by beta-galactosidase from Aspergillus oryzae" Process Biochemistry, 50, no. 5 (2015):782-788,
https://doi.org/10.1016/j.procbio.2015.01.028 .
