TY  - JOUR
AU  - Ahmed, Khaled S.O.H.
AU  - Milosavić, Nenad
AU  - Popović, Milica M.
AU  - Prodanović, Radivoje
AU  - Knežević, Zorica
AU  - Jankov, Ratko
PY  - 2007
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1111
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 ºC 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  - Maltaza iz S. cerevisiae je kovalentno imobilizovana na Sepabeads EC-EA nakon aktivacije nosača rastvorom glutaraldehida. Ispitivanjem kinetike imobilizacije utvrđeno je da se 25 % enzima imobilizuje nakon 24 časa. Imobilizovana α-glukozidaza ima isti pH optimum kao i rastvorni enzim, dok je optimalna temperatura za aktivnost imobilizovanog enzima uvećana za 10 °C u poređenju sa rastvornim enzimom. Kada se uporede zaostale aktivnosti rastvorne i imobilizovane forme α-glukozidaze, nakon inkubacije od 1 h na 45 °C rastvorni enzim ne pokazuje aktivnost dok imobilizovana forma zadržava oko 20 % početne aktivnosti. Imobilizovana forma enzima zadržava 20 % početne aktivnosti čak i posle 3 h inkubacije na 45 °C.
PB  - Serbian Chemical Society, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae
T1  - Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae
EP  - 1263
IS  - 12
SP  - 1255
VL  - 72
UR  - https://hdl.handle.net/21.15107/rcub_technorep_1111
ER  - 

@article{
author = "Ahmed, Khaled S.O.H. and Milosavić, Nenad and Popović, Milica M. and Prodanović, Radivoje and Knežević, Zorica and Jankov, Ratko",
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 ºC 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., Maltaza iz S. cerevisiae je kovalentno imobilizovana na Sepabeads EC-EA nakon aktivacije nosača rastvorom glutaraldehida. Ispitivanjem kinetike imobilizacije utvrđeno je da se 25 % enzima imobilizuje nakon 24 časa. Imobilizovana α-glukozidaza ima isti pH optimum kao i rastvorni enzim, dok je optimalna temperatura za aktivnost imobilizovanog enzima uvećana za 10 °C u poređenju sa rastvornim enzimom. Kada se uporede zaostale aktivnosti rastvorne i imobilizovane forme α-glukozidaze, nakon inkubacije od 1 h na 45 °C rastvorni enzim ne pokazuje aktivnost dok imobilizovana forma zadržava oko 20 % početne aktivnosti. Imobilizovana forma enzima zadržava 20 % početne aktivnosti čak i posle 3 h inkubacije na 45 °C.",
publisher = "Serbian Chemical Society, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae, Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae",
pages = "1263-1255",
number = "12",
volume = "72",
url = "https://hdl.handle.net/21.15107/rcub_technorep_1111"
}

Ahmed, K. S.O.H., Milosavić, N., Popović, M. M., Prodanović, R., Knežević, Z.,& Jankov, R.. (2007). Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society
Serbian Chemical Society, Belgrade., 72(12), 1255-1263.
https://hdl.handle.net/21.15107/rcub_technorep_1111

Ahmed KS, Milosavić N, Popović MM, Prodanović R, Knežević Z, Jankov R. Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society. 2007;72(12):1255-1263.
https://hdl.handle.net/21.15107/rcub_technorep_1111 .

Ahmed, Khaled S.O.H., Milosavić, Nenad, Popović, Milica M., Prodanović, Radivoje, Knežević, Zorica, Jankov, Ratko, "Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae" in Journal of the Serbian Chemical Society, 72, no. 12 (2007):1255-1263,
https://hdl.handle.net/21.15107/rcub_technorep_1111 .