Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by beta-galactosidase from Aspergillus oryzae
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2015
Authors
Simović, MilicaVeličković, Dušan
Stojanović, Marija
Milosavić, Nenad
Rogniaux, Helene
Ropartz, David
Bezbradica, Dejan
Article (Published version)
Metadata
Show full item recordAbstract
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 mobilitySource:
Process Biochemistry, 2015, 50, 5, 782-788Publisher:
- 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-MESTD-Integrated and Interdisciplinary Research (IIR or III)-46010)
- Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (RS-MESTD-Basic Research (BR or ON)-172049)
DOI: 10.1016/j.procbio.2015.01.028
ISSN: 1359-5113
WoS: 000354147700012
Scopus: 2-s2.0-84939994103
Institution/Community
Tehnološko-metalurški fakultetTY - 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", 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. in 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. in Process Biochemistry. 2015;50(5):782-788. doi:10.1016/j.procbio.2015.01.028 .
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 . .