Purification and characteristics of creatininase from Arthrobacter sp.
- Author:
Geng-Feng ZHAO
1
;
Xiao-Hang MA
;
Xiao-Ming JIA
;
Yu-Hua ZHAO
;
Yuan-Yuan WANG
Author Information
1. College of Life Sciences, Zhejiang University, Hangzhou 310029, China.
- Publication Type:Journal Article
- MeSH:
Amidohydrolases;
isolation & purification;
metabolism;
Arthrobacter;
enzymology;
Bacterial Proteins;
isolation & purification;
metabolism;
Chromatography, DEAE-Cellulose;
methods
- From:
Chinese Journal of Biotechnology
2005;21(2):250-253
- CountryChina
- Language:Chinese
-
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+.
