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A Journal on Biotechnology and Molecular Biology
Indexed/Abstracted in: EMBASE, Science Citation Index Expanded (SciSearch), Scopus
Impact Factor 0,246
Minerva Biotecnologica 2014 December;26(4):281-6
Increased expression of recombinant cholesterol oxidase in Escherichia coli by optimization of culture condition using response surface methodology
Moradpour Z. 1, Ghasemian A. 1, 2, Nouri F. 1, 2, Ghasemi Y. 1, 2
1 Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Urmia University of Medical Sciences, Urmia, Iran;
2 Pharmaceutical Sciences Research Center, Faculty of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran
AIM: The FAD-containing enzyme, cholesterol oxidase (EC 18.104.22.168) is an enzyme that catalyses sequential reactions which convert cholesterol (5-cholesten-3-b-ol) to 4-cholesten-3-one with concomitant reduction of oxygen to hydrogen peroxide. In fact, this enzyme catalyzes two reactions in one active site: oxidation and isomerization. Cholesterol oxidase is an industrially and commercially important enzyme.
METHODS: Response surface methodology that uses quantitative data from appropriate experiments was applied to optimize the culture conditions for recombinant cholesterol oxidase production in Escherichia coli (E. coli). Parameters considered were concentrations of IPTG, induction time, fermentation temperature and incubation period. Design of optimal experimental conditions was performed by four-factor, three levels Box-Behnken model which yielded improved cholesterol oxidase production.
RESULTS: Under optimal condition, productivity of cholesterol oxidase increased approximately 2-fold as compared to un-optimized medium.
CONCLUSION: These findings demonstrate that response surface methodology could efficiently be applied for optimization of recombinant cholesterol oxidase production in E. coli as the experimental data for productivity of cholesterol oxidase had a good correlation with predicted values.