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Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae
Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae
dc.creator | Ahmed, Khaled S.O.H. | |
dc.creator | Milosavić, Nenad | |
dc.creator | Popović, Milica M. | |
dc.creator | Prodanović, Radivoje | |
dc.creator | Knežević, Zorica | |
dc.creator | Jankov, Ratko | |
dc.date.accessioned | 2021-03-10T10:44:36Z | |
dc.date.available | 2021-03-10T10:44:36Z | |
dc.date.issued | 2007 | |
dc.identifier.issn | 0352-5139 | |
dc.identifier.uri | http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1111 | |
dc.description.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. | en |
dc.description.abstract | 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. | sr |
dc.publisher | Serbian Chemical Society, Belgrade | |
dc.relation | info:eu-repo/grantAgreement/MESTD/MPN2006-2010/142020/RS// | |
dc.rights | openAccess | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.source | Journal of the Serbian Chemical Society | |
dc.subject | maltase | en |
dc.subject | Sepabeads EC-EA | en |
dc.subject | immobilization | en |
dc.subject | stabilization | en |
dc.title | Preparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiae | en |
dc.title | Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae | sr |
dc.type | article | |
dc.rights.license | BY-NC-ND | |
dc.citation.epage | 1263 | |
dc.citation.issue | 12 | |
dc.citation.other | 72(12): 1255-1263 | |
dc.citation.rank | M23 | |
dc.citation.spage | 1255 | |
dc.citation.volume | 72 | |
dc.identifier.fulltext | http://TechnoRep.tmf.bg.ac.rs/bitstream/id/10588/0352-51390712255A.pdf | |
dc.identifier.rcub | https://hdl.handle.net/21.15107/rcub_technorep_1111 | |
dc.identifier.scopus | 2-s2.0-36949023795 | |
dc.identifier.wos | 000252412100009 | |
dc.type.version | publishedVersion |