Characterization of β-galactosidase immobilized into poly(hydroxyethylmethacrylate) membranes

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dc.cont.department-temp
dc.contributor.authorAdali, O
dc.contributor.authorBaran, T
dc.contributor.authorArica, MY
dc.date.accessioned2020-06-25T17:34:37Z
dc.date.available2020-06-25T17:34:37Z
dc.date.issued1998
dc.departmentKırıkkale Üniversitesi
dc.descriptionBaran, Erkan/0000-0002-0563-6943; Baran, Erkan/0000-0002-0563-6943
dc.description.abstractbeta-galactosidase was immobilized into pHEMA membranes with the highest specific activity yield of 9.5%. The specific activity of the entrapped enzyme was found to be decreased as the enzyme loading increased in pHEMA membranes. The optimum pH and temperature for maximum activity of the immobilized beta-galactosidase was found to be at pH 7.5 and 50 degrees C, respectively, and were the same as native enzyme. K-m and V-max values for the free enzyme were found to be 0.256 mM and 26.6 mu mole/min/mg, respectively. K-m value of immobilized beta-galactosidase was found to be increased about 3 folds upon immobilization. Operational, thermal and storage stability of beta-galactosidase were found to increase with immobilization. Immobilized enzyme preparation was reused in 15 cycles without significant loss in activity.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.endpage129en_US
dc.identifier.issn0749-5331
dc.identifier.issue2en_US
dc.identifier.startpage123en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12587/2802
dc.identifier.volume14en_US
dc.identifier.wosWOS:000075045300005
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.language.isoen
dc.publisherMbr Press Incen_US
dc.relation.ispartofBiochemical Archives
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectbeta-galactosidaseen_US
dc.subjectimmobilizationen_US
dc.titleCharacterization of β-galactosidase immobilized into poly(hydroxyethylmethacrylate) membranesen_US
dc.typeArticle

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