کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
9616759 48871 2005 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Comparative study of the properties of wild type and recombinant cyclohexanone monooxygenase, an enzyme of synthetic interest
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی کاتالیزور
پیش نمایش صفحه اول مقاله
Comparative study of the properties of wild type and recombinant cyclohexanone monooxygenase, an enzyme of synthetic interest
چکیده انگلیسی
Cyclohexanone monooxygenase (CHMO), a flavoenzyme of synthetic interest (it catalyses the NADPH-dependent enantioselective oxidation of ketones and of several heteroatoms such as nitrogen, sulfur, phosphorous and selenium present in organic compounds) previously overexpressed in E. coli (TOP10 pQR239), was purified to homogeneity, as demonstrated by SDS-PAGE and MALDI/TOF analysis, and characterised. The recombinant and the wild type (Acinetobacter) enzymes had identical molecular mass, Km values, pH-activity profile and circular dichroism spectra, but slightly differed for pH- and thermo-stability. The latter findings might be due to a different pattern of proteases contaminating the monooxygenases isolated from the two microorganims.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 34, Issues 1–6, 1 July 2005, Pages 1-6
نویسندگان
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