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Optimizacija esterifikacione aktivnosti lipaze iz Candida rugosa imobilisane mikrotalasnim zračenjem

dc.creatorMihailović, Mladen
dc.creatorKnežević-Jugović, Zorica
dc.creatorMijin, Dušan
dc.creatorBezbradica, Dejan
dc.date.accessioned2021-03-10T11:47:25Z
dc.date.available2021-03-10T11:47:25Z
dc.date.issued2012
dc.identifier.issn0367-598X
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/2081
dc.description.abstractLipases are very efficient biocatalysts with wide application in synthesis of important ingredients of food, cosmetics and pharmaceutical products, due to their capacity to catalyze both, ester synthesis and ester hydrolysis. The preparation of stable and active immobilized derivatives of lipases is necessity for their application in industrial enzymatic processes. In this work, the optimization of lipase from C. rugosa immobilization by microwave irradiation was performed, since it was previously reported that immobilization process can be drastically accelerated by means of microwave irradiation, even resulting with slight increase of lipase activity. Eupergit®, commercial support with active epoxy groups, was used as immobilization support. In first stage of our study, the immobilization time and ionic strength of immobilization buffer were optimized. It was found out that the highest immobilized activity can be achieved at high ionic strengths (1 M buffer) after 3 min, while further increase of immobilization time led to decrease of lipase activity. Then, the immobilized derivative obtained at optimum conditions was applied in synthesis of amyl isobutyrate in organic solvent. Key reaction factors (temperature, water concentration, immobilized lipase concentration, and substrate molar ratio) were optimized using response surface methodology. The substrate conversion higher above 85% was achieved in our study. The statistical analysis revealed that each of analyzed factors had significant effect on yield of ester, with initial enzyme concentration and substrate molar ratio being the most prominent factors. The second-order regression model that describes the effect of all four factors on substrate conversion was established. The optimum values of factors were: temperature 50°C, initial immobilized enzyme concentration 220 mg ml-1, added water concentration 0.1% (v/v), and molar ratio acid/alcohol 2.5.en
dc.description.abstractLipaze su enzimi koji imaju široku primenu u prehrambenoj, kozmetičkoj i farmaceutskoj industriji. U industrijskoj praksi primenjuju se imobilisane lipaze jer se imobilizacijom povećava njihova stabilnost i ekonomičnost enzimskih postupaka. U ovom radu optimizovana je imobilizacija lipaze iz C. rugosa na komercijalni nosač Eupergit® pomoću mikrotalasnog zračenja. Vreme izlaganja mikrotalasima i molaritet korišćenog pufera optimizovani su sa ciljem dobijanja imobilizata maksimalne aktivnosti. Radi optimizovanja reakcije sinteze amil-izobutirata, pomoću centralnog kompozitnog rotatabilnog plana ispitan je uticaj četiri reakciona faktora. Ustanovljeno je da su optimalni uslovi sinteze estra temperatura 50°C, početna koncentracija imobilisanog enzima 220 mg ml-1, koncentracija dodate vode 0,1% i molarni odnos supstrata 2,5.sr
dc.publisherAssociation of Chemical Engineers of Serbia
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172013/RS//
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceHemijska industrija
dc.subjectmicrowaveen
dc.subjectEupergit®en
dc.subjectimmobilizationen
dc.subjectlipaseen
dc.subjectmikrotalasisr
dc.subjectEupergit®sr
dc.subjectimobilizacijasr
dc.subjectlipazasr
dc.titleOptimization of esterification activity of lipase from Candida rugosa immobilized using microwave irradiationen
dc.titleOptimizacija esterifikacione aktivnosti lipaze iz Candida rugosa imobilisane mikrotalasnim zračenjemsr
dc.typearticle
dc.rights.licenseBY-NC-ND
dc.citation.epage19
dc.citation.issue1
dc.citation.other66(1): 9-19
dc.citation.rankM23
dc.citation.spage9
dc.citation.volume66
dc.identifier.doi10.2298/HEMIND110720060M
dc.identifier.fulltexthttp://TechnoRep.tmf.bg.ac.rs/bitstream/id/8935/0367-598X1201009M.pdf
dc.identifier.scopus2-s2.0-84859074647
dc.identifier.wos000311594000002
dc.type.versionpublishedVersion


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