سال انتشار: ۱۳۸۶

محل انتشار: پنجمین کنگره بین المللی مهندسی شیمی

تعداد صفحات: ۹

نویسنده(ها):

Bahrami – Biotechnology Group, Chemical Engineering Department, Faculty of Engineering, Tarbiat Modarres University, Tehran, Iran
Shojaosadati – Biotechnology Group, Chemical Engineering Department, Faculty of Engineering, Tarbiat Modarres University, Tehran,Iran
Khalilzadeh – Institute of Biotechnology, Malek Ashtar University, Tehran, I.R. Iran.
Vasheghani Farahani – Biotechnology Group, Chemical Engineering Department, Faculty of Engineering, Tarbiat Modarres University, Tehran,Iran

چکیده:

The methylotrophic yeast Pichia pastoris is a powerful system for production of recombinant proteins, showing high ability to secrete properly folded proteins. A major plus is the strong AOX1 promoter highly induced by methanol. The optimal culture conditions for attaining high cell density and expression of human Granulocyte-Colony Stimulating Factor (hG-CSF) in the Pichia pastoris were investigated. Cell growth and hG-CSF production were found to be optimal at temperature of 28 °C and pH of 6.0. By using the three stages fermentation, final dry cell weight and expression of recombinant hG-CSF in a fed-batch culture was reached to 90 g/l and 20 mg/l, respectively. Dry cell density and recombinant protein secretion capacity were increased to 100 g/l and 40 mg/l by feeding of peptone as nitrogen source in the methanol induction phase. This study demonstrates that addition of the appropriate amount of an organic nitrogen source to the fed-batch culture is effective to improve expression of recombinant protein in the methylotrophic yeast P. pastoris.