Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae
Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae
2007
Аутори
Ahmedi, Khaled S. O. H.Milosaviz, Nenad B.
Popović, Milica M.
Prodanović, Radivoje
Knezevic, Zorica D.
Jankov, Ratko M.
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
alpha-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 alpha-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 degrees 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 r...eproducible and provides a promising solution for the application of immobilized alpha-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.
Кључне речи:
maltase / Sepabeads EC-EA / Sepabeads EC-EA / immobilization / immobilization / stabilization / stabilizationИзвор:
Journal of the Serbian Chemical Society, 2007, 72, 12, 1255-1263Издавач:
- Serbian Chemical Soc, Belgrade
Финансирање / пројекти:
- Испитивање структуре и функције биолошки важних макромолекула у физиолошким и патолошким стањима (RS-MESTD-MPN2006-2010-142020)
DOI: 10.2298/JSC0712255A
ISSN: 0352-5139
WoS: 000252412100009
Scopus: 2-s2.0-36949023795
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Ahmedi, Khaled S. O. H. AU - Milosaviz, Nenad B. AU - Popović, Milica M. AU - Prodanović, Radivoje AU - Knezevic, Zorica D. AU - Jankov, Ratko M. PY - 2007 UR - https://cherry.chem.bg.ac.rs/handle/123456789/904 AB - alpha-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 alpha-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 degrees 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 alpha-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 Soc, Belgrade T2 - Journal of the Serbian Chemical Society T1 - Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae T1 - Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae VL - 72 IS - 12 SP - 1255 EP - 1263 DO - 10.2298/JSC0712255A ER -
@article{ author = "Ahmedi, Khaled S. O. H. and Milosaviz, Nenad B. and Popović, Milica M. and Prodanović, Radivoje and Knezevic, Zorica D. and Jankov, Ratko M.", year = "2007", abstract = "alpha-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 alpha-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 degrees 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 alpha-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 Soc, Belgrade", journal = "Journal of the Serbian Chemical Society", title = "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae, Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae", volume = "72", number = "12", pages = "1255-1263", doi = "10.2298/JSC0712255A" }
Ahmedi, K. S. O. H., Milosaviz, N. B., Popović, M. M., Prodanović, R., Knezevic, 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 Serbian Chemical Soc, Belgrade., 72(12), 1255-1263. https://doi.org/10.2298/JSC0712255A
Ahmedi KSOH, Milosaviz NB, Popović MM, Prodanović R, Knezevic 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., Milosaviz, Nenad B., Popović, Milica M., Prodanović, Radivoje, Knezevic, 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 . .