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Properties of alkaline protease genetically engineered on cell surface of the yeast Yarrowia lipolytica.
Indian J Biochem Biophys ; 2009 Aug; 46(4): 294-298
Article in English | IMSEAR | ID: sea-135208
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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Full text: Available Index: IMSEAR (South-East Asia) Main subject: Endopeptidases / Temperature / Bacterial Proteins / Kinetics / Caseins / Genetic Engineering / Cations / Gene Expression Regulation, Fungal / Cell Membrane / Cloning, Molecular Language: English Journal: Indian J Biochem Biophys Year: 2009 Type: Article

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Full text: Available Index: IMSEAR (South-East Asia) Main subject: Endopeptidases / Temperature / Bacterial Proteins / Kinetics / Caseins / Genetic Engineering / Cations / Gene Expression Regulation, Fungal / Cell Membrane / Cloning, Molecular Language: English Journal: Indian J Biochem Biophys Year: 2009 Type: Article