Biochemical properties of penicillin amidohydrolase from Micrococcus luteus

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Biochemical properties of penicillin amidohydrolase from Micrococcus luteus.

Some biochemical properties of whole-cell penicillin amidohydrolase from Micrococcus luteus have been studied. This whole-cell enzyme showed its maximal activity at 36 degrees C at pH 7.5. It was found that the activation energy of this enzyme was 8.03 kcal (ca. 33.6 kJ) per mol, and this amidohydrolase showed first-order decay at 36 degrees C. The penicillin amidohydrolase was deactivated rapi...

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DNA-relaxing enzyme from Micrococcus luteus.

A DNA-relaxing enzyme which catalyzes the conversion of superhelical DNA to a non-superhelical covalently closed form has been purified from Micrococcus luteus to near homogeneity by two chromatographic steps. The enzyme is a single polypeptide chain. As determined by sodium dodecyl sulfate - polyacrylamide gel electrophoresis and gel filtration on Sephadex G 150, the molecular weight is 115,00...

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Keratinolytic abilities of Micrococcus luteus from poultry waste

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Degradation of Pyridine by Micrococcus luteus Isolated from Soil.

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ژورنال

عنوان ژورنال: Applied and Environmental Microbiology

سال: 1979

ISSN: 0099-2240,1098-5336

DOI: 10.1128/aem.38.1.35-38.1979