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Yazdi MT, Zahraei M, Aghaepour K, et al. Purification and partial characterization of a cholesterol oxidase from Streptomyces fradiae. Enzyme Microb Technol. 2001;28(4):410-414doi: 10.1016/s0141-0229(00)00337-9.
Yazdi, M. T., Zahraei, M., Aghaepour, K., & Kamranpour, N. (2001). Purification and partial characterization of a cholesterol oxidase from Streptomyces fradiae. Enzyme and microbial technology, 28(4), 410-414. https://doi.org/10.1016/s0141-0229(00)00337-9
Yazdi, M T., et al. "Purification and partial characterization of a cholesterol oxidase from Streptomyces fradiae." Enzyme and microbial technology vol. 28,4 (2001): 410-414. doi: https://doi.org/10.1016/s0141-0229(00)00337-9
Yazdi MT, Zahraei M, Aghaepour K, Kamranpour N. Purification and partial characterization of a cholesterol oxidase from Streptomyces fradiae. Enzyme Microb Technol. 2001 Mar 08;28(4):410-414. doi: 10.1016/s0141-0229(00)00337-9. PMID: 11240199.
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Enzyme Microb Technol. 2001 Mar 08;28(4):410-414. doi: 10.1016/s0141-0229(00)00337-9.

Purification and partial characterization of a cholesterol oxidase from Streptomyces fradiae.

Enzyme and microbial technology

M T. Yazdi, M Zahraei, K Aghaepour, N Kamranpour

Affiliations

  1. Department of Biotechnology, College of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran

PMID: 11240199 DOI: 10.1016/s0141-0229(00)00337-9

Abstract

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.

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