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 Title |
: Expression of the Cholesterol Oxidase Gene in Escherichia coli M15 (pREP4) |
 Author |
: Potjamarn SURANINPONG |
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Co-authors |
: Sontichai CHANPRAME,Hyeon-Je CHO, Jack M. WIDHOLM and Aree WARANYUWAT |
 School |
: Walailak University |
 Department |
: |
 Source |
: Annual Research Abstracts 2002-2003 |
 Grant |
: Small Ruminant Research and Development Centre, Faculty of Natural Resources, Prince of Songkla University. |
 Knowledge Bank Category |
: Agriculture |
 Viewes |
: 433 |
 Abstract |
: ress vectors. The constructed vectors were transformed into Escherichia coli train M15 (pREP4) to express the choA gene. Determination of target protein of this bacterium showed an intracellular soluble protein. Crude cell lysate of a positive control M15 (pREP4) pCO117 showed much more enzyme activity (560 mU mg protein-1) than did the in-frame sequence M15 (pREP4) pQE30-choA (317 mU mg protein-1) and a negative control M15 (pREP4) pQE30 (9 mU mg-1 protein) after induction with IPTG. Time course analysis of the M15 (pREP4) pQE30-choA showed the highest activity after the cells were grown for 4 h with IPTG. Purified protein of this clone had a specific activity of 5.59 U mg-1 protein with a single band with the M.W. of 57 kDa. The production of cholesterol oxidase protein in this bacterium appeared to be influenced by various factors such as media, culture conditions, density of bacterial cells, IPTG concentrations, and enzyme assay methods. |
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