Galacto-oligosaccharide synthesis using chemically modified beta-galactosidase from Aspergillus oryzae immobilised onto macroporous amino resin
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2016
Authors
Simović, MilicaĆorović, Marija
Mihailović, Mladen
Banjanac, Katarina
Milivojević, Ana
Veličković, Dušan
Bezbradica, Dejan
Article (Published version)
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The goal of this study was to establish an efficient immobilisation protocol for beta-galactosidase from Aspergillus oryzae onto the polystyrenic macroporous resin Purolite (R) A-109 for better utilisation of its transglactosylation activity and application in galacto-oligosaccharide (GOS) synthesis. This was achieved by improving simple ionic adsorption by carboxyl group activation on the enzyme surface with carbodiimide, enabling covalent immobilisation. This yielded significantly increased operational stability, assayed as GOS synthesis, in a batch reactor, and even more prominently, in a fluidised bed reactor (73% activity retained after 10 cycles). The immobilised enzyme showed two very beneficial advantages over the free enzyme for future applications: higher affinity towards catalysing transgalactosylation than towards hydrolysis and shift of pH optimum towards more acidic conditions. GOS synthesis performed under the optimum conditions obtained (400 g L-1 lactose, pH 4.5, 50 de...grees C) yielded 87 g L-1 and 100 g L-1 for batch and fluidised bed reactors, respectively.
Source:
International Dairy Journal, 2016, 54, 50-57Publisher:
- 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)
DOI: 10.1016/j.idairyj.2015.10.002
ISSN: 0958-6946
WoS: 000368021400007
Scopus: 2-s2.0-84949845593
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Tehnološko-metalurški fakultetTY - JOUR AU - Simović, Milica AU - Ćorović, Marija AU - Mihailović, Mladen AU - Banjanac, Katarina AU - Milivojević, Ana AU - Veličković, Dušan AU - Bezbradica, Dejan PY - 2016 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3374 AB - The goal of this study was to establish an efficient immobilisation protocol for beta-galactosidase from Aspergillus oryzae onto the polystyrenic macroporous resin Purolite (R) A-109 for better utilisation of its transglactosylation activity and application in galacto-oligosaccharide (GOS) synthesis. This was achieved by improving simple ionic adsorption by carboxyl group activation on the enzyme surface with carbodiimide, enabling covalent immobilisation. This yielded significantly increased operational stability, assayed as GOS synthesis, in a batch reactor, and even more prominently, in a fluidised bed reactor (73% activity retained after 10 cycles). The immobilised enzyme showed two very beneficial advantages over the free enzyme for future applications: higher affinity towards catalysing transgalactosylation than towards hydrolysis and shift of pH optimum towards more acidic conditions. GOS synthesis performed under the optimum conditions obtained (400 g L-1 lactose, pH 4.5, 50 degrees C) yielded 87 g L-1 and 100 g L-1 for batch and fluidised bed reactors, respectively. PB - Elsevier Sci Ltd, Oxford T2 - International Dairy Journal T1 - Galacto-oligosaccharide synthesis using chemically modified beta-galactosidase from Aspergillus oryzae immobilised onto macroporous amino resin EP - 57 SP - 50 VL - 54 DO - 10.1016/j.idairyj.2015.10.002 ER -
@article{ author = "Simović, Milica and Ćorović, Marija and Mihailović, Mladen and Banjanac, Katarina and Milivojević, Ana and Veličković, Dušan and Bezbradica, Dejan", year = "2016", abstract = "The goal of this study was to establish an efficient immobilisation protocol for beta-galactosidase from Aspergillus oryzae onto the polystyrenic macroporous resin Purolite (R) A-109 for better utilisation of its transglactosylation activity and application in galacto-oligosaccharide (GOS) synthesis. This was achieved by improving simple ionic adsorption by carboxyl group activation on the enzyme surface with carbodiimide, enabling covalent immobilisation. This yielded significantly increased operational stability, assayed as GOS synthesis, in a batch reactor, and even more prominently, in a fluidised bed reactor (73% activity retained after 10 cycles). The immobilised enzyme showed two very beneficial advantages over the free enzyme for future applications: higher affinity towards catalysing transgalactosylation than towards hydrolysis and shift of pH optimum towards more acidic conditions. GOS synthesis performed under the optimum conditions obtained (400 g L-1 lactose, pH 4.5, 50 degrees C) yielded 87 g L-1 and 100 g L-1 for batch and fluidised bed reactors, respectively.", publisher = "Elsevier Sci Ltd, Oxford", journal = "International Dairy Journal", title = "Galacto-oligosaccharide synthesis using chemically modified beta-galactosidase from Aspergillus oryzae immobilised onto macroporous amino resin", pages = "57-50", volume = "54", doi = "10.1016/j.idairyj.2015.10.002" }
Simović, M., Ćorović, M., Mihailović, M., Banjanac, K., Milivojević, A., Veličković, D.,& Bezbradica, D.. (2016). Galacto-oligosaccharide synthesis using chemically modified beta-galactosidase from Aspergillus oryzae immobilised onto macroporous amino resin. in International Dairy Journal Elsevier Sci Ltd, Oxford., 54, 50-57. https://doi.org/10.1016/j.idairyj.2015.10.002
Simović M, Ćorović M, Mihailović M, Banjanac K, Milivojević A, Veličković D, Bezbradica D. Galacto-oligosaccharide synthesis using chemically modified beta-galactosidase from Aspergillus oryzae immobilised onto macroporous amino resin. in International Dairy Journal. 2016;54:50-57. doi:10.1016/j.idairyj.2015.10.002 .
Simović, Milica, Ćorović, Marija, Mihailović, Mladen, Banjanac, Katarina, Milivojević, Ana, Veličković, Dušan, Bezbradica, Dejan, "Galacto-oligosaccharide synthesis using chemically modified beta-galactosidase from Aspergillus oryzae immobilised onto macroporous amino resin" in International Dairy Journal, 54 (2016):50-57, https://doi.org/10.1016/j.idairyj.2015.10.002 . .