Properties of alkaline protease genetically engineered on cell surface of the yeast Yarrowia lipolytica.
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Date
2009-08
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Abstract
ALP2 gene encoding alkaline protease cloned from Aureobasidium pullulans HN2-3 was ligated into the surface display plasmid and expressed in the cells of the yeast Yarrowia lipolytica. The expressed alkaline protease was immobilized on the yeast cells. The activity of the immobilized enzyme with 6 His tag was found to be significantly higher than that of without 6 His tag. The immobilized enzyme showed lower optimal temperature and a lower affinity for azocasein than the free enzyme purified from A. pullulans HN2-3. The thermal stability of the immobilized enzyme enhanced and the pH stability decreased, compared to that of the free enzyme.
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Keywords
Yeast surface display, Alkaline protease, Aureobasidium pullulans, Yarrowia lipolytica, Marine yeast
Citation
Ni Xiumei, Yue Lixi, Li Jing, Chi Zhenming, Liu Zhiqiang, Madzak Catherine. Properties of alkaline protease genetically engineered on cell surface of the yeast Yarrowia lipolytica. Indian Journal of Biochemistry & Biophysics. 2009 Aug; 46(4): 294-298.