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Immobilization of dill (Anethum Graveolens L.) catalase and its properties

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dc.contributor.authors Arabaci, G; Usluoglu, A;
dc.date.accessioned 2020-02-24T14:15:01Z
dc.date.available 2020-02-24T14:15:01Z
dc.date.issued 2012
dc.identifier.citation Arabaci, G; Usluoglu, A; (2012). Immobilization of dill (Anethum Graveolens L.) catalase and its properties. ASIA-PACIFIC JOURNAL OF CHEMICAL ENGINEERING, 7, S300-S296
dc.identifier.issn 1932-2135
dc.identifier.uri https://doi.org/10.1002/apj.1647
dc.identifier.uri https://hdl.handle.net/20.500.12619/44832
dc.description.abstract Over the last decade, enzyme immobilization has become more important in industry and biotechnology. In this study, catalase from dill (Anethum graveolens L.) plant was immobilized covalently with glutaraldehyde onto chitosan particles. The pH and temperature optima as well as the changes in the kinetics of the immobilized and free dill catalase were determined. The K-m value for immobilized catalase (35 mM) was higher about 1.5-fold than that of free enzyme (24 mM). Optimum temperature was observed at 40 degrees C, a 10 degrees C higher than that of the free enzyme and was significantly broader. The optimum pH was same for both free and immobilized catalase (pH 7.0). Immobilized catalase showed higher storage stabilities than free catalase. Thermal stability increased with immobilization. Free catalase lost all its activity, whereas immobilized catalase lost 45% of its activity within 60 days incubation period at 4 degrees C. Free catalase lost all its activity within 5 days, whereas immobilized catalase lost 65% of its activity within 60 days at 25 degrees C. The remaining activity of the catalase was about 70% after 10 cycles of batch operation. It was observed that operational, thermal and storage stabilities of the enzyme increased with immobilization. (c) 2012 Curtin University of Technology and John Wiley & Sons, Ltd.
dc.language English
dc.publisher WILEY-BLACKWELL
dc.subject Engineering
dc.title Immobilization of dill (Anethum Graveolens L.) catalase and its properties
dc.type Article
dc.identifier.volume 7
dc.identifier.startpage S296
dc.identifier.endpage S300
dc.contributor.department Sakarya Üniversitesi/Fen-Edebiyat Fakültesi/Kimya Bölümü
dc.contributor.saüauthor Arabacı, Gülnur
dc.relation.journal ASIA-PACIFIC JOURNAL OF CHEMICAL ENGINEERING
dc.identifier.wos WOS:000209130300007
dc.identifier.doi 10.1002/apj.1647
dc.identifier.eissn 1932-2143
dc.contributor.author Arabacı, Gülnur


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