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Dobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiae

dc.creatorAhmed, Khaled S.O.H.
dc.creatorMilosavić, Nenad
dc.creatorPopović, Milica M.
dc.creatorProdanović, Radivoje
dc.creatorKnežević, Zorica
dc.creatorJankov, Ratko
dc.date.accessioned2021-03-10T10:44:36Z
dc.date.available2021-03-10T10:44:36Z
dc.date.issued2007
dc.identifier.issn0352-5139
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/1111
dc.description.abstractα-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.abstractMaltaza 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.publisherSerbian Chemical Society, Belgrade
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceJournal of the Serbian Chemical Society
dc.subjectmaltaseen
dc.subjectSepabeads EC-EAen
dc.subjectimmobilizationen
dc.subjectstabilizationen
dc.titlePreparation and studies on immobilized α-glucosidase from baker’s yeast Saccharomyces cerevisiaeen
dc.titleDobijanje i proučavanje imobilizacije α-glukozidaze iz pekarskog kvasca Saccharomyces cerevisiaesr
dc.typearticle
dc.rights.licenseBY-NC-ND
dc.citation.epage1263
dc.citation.issue12
dc.citation.other72(12): 1255-1263
dc.citation.rankM23
dc.citation.spage1255
dc.citation.volume72
dc.identifier.rcubconv_628
dc.identifier.scopus2-s2.0-36949023795
dc.identifier.wos000252412100009
dc.type.versionpublishedVersion


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