Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/3363
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dc.contributor.advisorHarsa, Hayriye Şebnemen
dc.contributor.authorÇabuk, Burcu-
dc.date.accessioned2014-07-22T13:51:23Z
dc.date.available2014-07-22T13:51:23Z
dc.date.issued2008en
dc.identifier.urihttp://hdl.handle.net/11147/3363
dc.descriptionThesis (Master)--Izmir Institute of Technology, Food Engineering, Izmir, 2008en
dc.descriptionIncludes bibliographical references (leaves: 66-72)en
dc.descriptionText in English; Abstract: Turkish and Englishen
dc.descriptionxiii, 75 106 leavesen
dc.description.abstractB-galactosidase (lactase) enzyme is of great industrial interest, since it can be used to solve problems associated with whey disposal and lactose crystallization in sweetened and frozen dairy products such as ice cream. All over the world, many people suffer from lactose intolerance and lactase preparations are used as supplements for these persons. B-galactosidase is also used to produce prebiotics since this enzyme hydrolyses lactose into galactooligosaccharides. Immobilized B-galactosidase preparations are preferred in many processes because they can be recycled and maintain their activities for a long time without loosing their chemical stability.Novel cross-linked chitosan-hydroxyapatite composite support has beenprepared, lactase from Kluyveromyces lactis was immobilized onto these beads. Lactase immobilization mechanism and effect of factors such as initial glutaraldehyde concentration, temperature, pH, initial lactase concentration, solid-liquid ratio on immobilzation mechanism were studied.Optimum cross-linking was obtained at the glutaraldehyde concentration of 100 mg/L. The optimum values of temperature, pH and solid/liquid ratio on lactase/HAChitosan were found to be 200C, pH 7.5 and 0.3g/ml Vg/Vl, respectively. The pH and thermal stabilities of free and immobilized enzymes were also investigated and it was observed that the relative activity remained above 83.2% within pH 6-7.5 and maximum activity yield was obtained at 370C for free and all immobilized enzymes. The Michaelis constant Km and Vmax of immobilized and free enzyme on chitosanhydroxyapatite composite beads were found to be 9.5 mM and Vm 454.5 .mol ONP min.1 mg.1 protein and 1.011 mM and 1098.9 .mol ONP min.1 mg.1 protein, respectively.en
dc.language.isoenen_US
dc.publisherIzmir Institute of Technologyen
dc.publisherIzmir Institute of Technologyen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subject.lccQP609.63 C11 2008en
dc.subject.lcshBeta-galactosidaseen
dc.subject.lcshLactoseen
dc.subject.lcshLactose intoleranceen
dc.subject.lcshImmobilized enzymesen
dc.subject.lcshHydrolysisen
dc.titleB-galactosidase of kluyveromyces lactis: Immobilization, characterization and hydrolysis behavior of enzymeen_US
dc.typeMaster Thesisen_US
dc.authoridTR116554
dc.institutionauthorÇabuk, Burcu-
dc.departmentIzmir Institute of Technology. Food Engineeringen
dc.departmentIzmir Institute of Technology. Food Engineeringen_US
dc.relation.publicationcategoryTezen_US
item.openairetypeMaster Thesis-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
item.fulltextWith Fulltext-
item.grantfulltextopen-
item.cerifentitytypePublications-
Appears in Collections:Master Degree / Yüksek Lisans Tezleri
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