Chemically Modified Sepharose as Support for the Immobilization of Cholesterol Oxidase
자연과학 > 생물
( Hai Lin Yang ) , ( Yi Chen ) , ( Yu Xin ) , ( Ling Zhang ) , ( Yu Ran Zhang ) , ( Wu Wang )
한국미생물생명공학회(구 한국산업미생물학회)
Journal of Microbiology and Biotechnology 2013년, 제23권 제9호, 1212~1220페이지(총9페이지)
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    Because the cholesterol oxidase from Brevibacterium sp. M201008 was not as stable as the free enzyme form, it had been covalently immobilized onto chemically modified Sepharose particles via N-ethyl-N`-3-dimethylaminopropyl carbodiimide. The optimum immobilization conditions were determined, and the immobilized enzyme activity obtained was 12.01 U/g Sepharose-ethylenediamine. The immobilization of the enzyme was characterized by Fourier transform infrared spectroscopy. The immobilized enzyme exhibited the maximal activity at 35oC and pH 7.5, which was unchanged compared with the free form. After being repeatedly used 20 times, the immobilized enzyme retained more than 40.43% of its original activity. The immobilized enzyme showed better operational stability, including wider thermal and pH ranges, and retained 62.87% activity after 20 days of storage at 4oC, which was longer than the free enzyme.
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