Purification and characteristics of creatininase from Arthrobacter sp / 生物工程学报
Chinese Journal of Biotechnology
; (12): 250-253, 2005.
Article
en Zh
| WPRIM
| ID: wpr-249916
Biblioteca responsable:
WPRO
ABSTRACT
A creatininase produced from a Arthrobacter sp. was purified 145-fold by a series of steps including heat treatment, ammonium sulfate precipitation, DEAE-Cellulose ion-exchange and hydrophobic chromatography. The specific activity of the pure enzyme was 209u/mg. The subunit molecular mass of creatininase was estimated to be 33 700D by SDS-PAGE. The creatininase was stable in the pH range between 6.0 - 9.0 and below 60 degrees C . Its Km value for creatinine was estimated to be 21.14 mmol/L. The enzyme was markedly inactivated by incubation with 1 mmol/L of Hg2+, Ag2+, Li+, Cu2+ and 20 mmol/L of 1, 11-Phananthroline respectively. Activation was observed when the enzyme was incubated with 1 mmol/L of Co2+ and Mn2+.
Texto completo:
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Índice:
WPRIM
Asunto principal:
Arthrobacter
/
Proteínas Bacterianas
/
Cromatografía DEAE-Celulosa
/
Amidohidrolasas
/
Metabolismo
/
Métodos
Idioma:
Zh
Revista:
Chinese Journal of Biotechnology
Año:
2005
Tipo del documento:
Article