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Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by beta-galactosidase from Aspergillus oryzae

Authorized Users Only
2015
Authors
Simović, Milica
Veličković, Dušan
Stojanović, Marija
Milosavić, Nenad
Rogniaux, Helene
Ropartz, David
Bezbradica, Dejan
Article (Published version)
Metadata
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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.
Keywords:
Salicin / beta-Galactosidase / Transgalactosylation / response surface methodology (RSM) / Ion mobility
Source:
Process Biochemistry, 2015, 50, 5, 782-788
Publisher:
  • Elsevier Sci Ltd, Oxford
Funding / projects:
  • Novel encapsulation and enzyme technologies for designing of new biocatalysts and biologically active compounds targeting enhancement of food quality, safety and competitiveness (RS-46010)
  • Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (RS-172049)

DOI: 10.1016/j.procbio.2015.01.028

ISSN: 1359-5113

WoS: 000354147700012

Scopus: 2-s2.0-84939994103
[ Google Scholar ]
17
15
URI
http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3018
Collections
  • Radovi istraživača / Researchers’ publications (TMF)
Institution/Community
Tehnološko-metalurški fakultet
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
UR  - conv_4722
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",
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",
url = "conv_4722"
}
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. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 50(5), 782-788.
https://doi.org/10.1016/j.procbio.2015.01.028
conv_4722
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. in Process Biochemistry. 2015;50(5):782-788.
doi:10.1016/j.procbio.2015.01.028
conv_4722 .
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" in Process Biochemistry, 50, no. 5 (2015):782-788,
https://doi.org/10.1016/j.procbio.2015.01.028 .,
conv_4722 .

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