Insight in the regioselective enzymatic transgalactosylation of salicin catalyzed by beta-galactosidase from Aspergillus oryzae
Samo za registrovane korisnike
2015
Autori
Simović, MilicaVeličković, Dušan
Stojanović, Marija
Milosavić, Nenad
Rogniaux, Helene
Ropartz, David
Bezbradica, Dejan
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Ključne reči:
Salicin / beta-Galactosidase / Transgalactosylation / response surface methodology (RSM) / Ion mobilityIzvor:
Process Biochemistry, 2015, 50, 5, 782-788Izdavač:
- Elsevier Sci Ltd, Oxford
Finansiranje / projekti:
- Razvoj novih inkapsulacionih i enzimskih tehnologija za proizvodnju biokatalizatora i biološki aktivnih komponenata hrane u cilju povećanja njene konkurentnosti, kvaliteta i bezbednosti (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-46010)
- Alergeni, antitela, enzimi i mali fiziološki značajni molekuli: dizajn, struktura, funkcija i značaj (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
Institucija/grupa
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 . .