Please use this identifier to cite or link to this item: http://earsiv.odu.edu.tr:8080/xmlui/handle/11489/2568
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dc.contributor.authorAlkan, Salih-
dc.contributor.authorTurgut, Umit-
dc.date.accessioned2022-08-17T06:46:19Z-
dc.date.available2022-08-17T06:46:19Z-
dc.date.issued2017-
dc.identifier.urifile:///C:/Users/test/Downloads/FEB_07_2017_Pp_4320-4901.pdf-
dc.identifier.urihttps://www.prt-parlar.de/download_feb_2017/-
dc.identifier.urihttp://earsiv.odu.edu.tr:8080/xmlui/handle/11489/2568-
dc.description.abstractThe properties of the clay kaolinite as a support for enzyme immobilization were studied using the enzyme lipase. Lipases are biocatalysts of great importance due to their ability to catalyze diverse reactions. They are extensively used for the catalysis in organic solvents, which leads to multiple industrial applications. Studies have been done at different (pH 4,0- 10,0) and in the temperature range of 20-80 degrees C. Taking into the account the Lagergren first-order equation for adsorption kinetics, q(1) and k(1) values, are a measure of absorbance strength were obtained. The values adsorption enthalpy (Delta H-0), Gibbs free enthalpy (Delta G(0)) and adsorption entropy (Delta S-0) were thermodynamics parameters. These studies indicate that kaolinite is a valuable support for the simple adsorption of enzymes.en_US
dc.language.isoengen_US
dc.publisherPARLAR SCIENTIFIC PUBLICATIONS (P S P), ANGERSTR. 12, 85354 FREISING, GERMANYen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectKaolinite; lipase enzyme; immobilization; adsorption; kineticen_US
dc.subjectREMOVALen_US
dc.titleANALYSIS OF ADSORPTION AND KINETIC OF LIPASE ENZYME ON KAOLINITEen_US
dc.typearticleen_US
dc.relation.journalFRESENIUS ENVIRONMENTAL BULLETINen_US
dc.contributor.departmentOrdu Üniversitesien_US
dc.identifier.volume26en_US
dc.identifier.issue7en_US
dc.identifier.startpage4416en_US
dc.identifier.endpage4419en_US
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