TY  - JOUR
AU  - Ahmedi, Khaled S. O. H
AU  - Milosavić, Nenad
AU  - Popović, Milica
AU  - Prodanović, Radivoje M.
AU  - Knežević-Jugović, Zorica D.
AU  - Jankov, Ratko M.
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4302
AB  - α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase.
AB  - Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae
T1  - Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae
VL  - 72
IS  - 12
SP  - 1255
EP  - 1263
DO  - 10.2298/JSC0712255A
ER  - 

@article{
author = "Ahmedi, Khaled S. O. H and Milosavić, Nenad and Popović, Milica and Prodanović, Radivoje M. and Knežević-Jugović, Zorica D. and Jankov, Ratko M.",
year = "2007",
abstract = "α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase., Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae, Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae",
volume = "72",
number = "12",
pages = "1255-1263",
doi = "10.2298/JSC0712255A"
}

Ahmedi, K. S. O. H., Milosavić, N., Popović, M., Prodanović, R. M., Knežević-Jugović, Z. D.,& Jankov, R. M.. (2007). Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 72(12), 1255-1263.
https://doi.org/10.2298/JSC0712255A

Ahmedi KSOH, Milosavić N, Popović M, Prodanović RM, Knežević-Jugović ZD, Jankov RM. Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society. 2007;72(12):1255-1263.
doi:10.2298/JSC0712255A .

Ahmedi, Khaled S. O. H, Milosavić, Nenad, Popović, Milica, Prodanović, Radivoje M., Knežević-Jugović, Zorica D., Jankov, Ratko M., "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae" in Journal of the Serbian Chemical Society, 72, no. 12 (2007):1255-1263,
https://doi.org/10.2298/JSC0712255A . .