Purification and partial characterization of a cholesterol oxidase from Streptomyces fradiae.
An extracellular cholesterol oxidase from Streptomyces fradiae (PTCC 1121) was purified in one step using DEAE-Sepharose. The purified enzyme had a molecular weight of 60 KDa. The optimum pH and temperature for activity was found to be 7 and 70 degrees C, respectively. This cholesterol oxidase was stable in pHs between 4-10 at 4 degrees C until 4 h. Thermal stability experiments showed that it has high stability and retains its full activity at 50 degrees C for 90 min. K(m) value for cholesterol oxidase was obtained to be about 7.06 x 10(-)(5) Mol.
Department of Biotechnology, College of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran
M T.
MT
Yazdi
M
M
Zahraei
K
K
Aghaepour
N
N
Kamranpour