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KMID : 0545120050150010202
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Journal of Microbiology and Biotechnology
2005 Volume.15 No. 1 p.202 ~ p.205
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Production of Active Carboxypeptidase Y of Saccharomyces cerevisiae Secreted from Methylotrophic Yeast Pichia pastoris
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Ro HS
Lee MS/Hahm MS/Bae HS/Chung BH
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Abstract
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Our previous study showed that the overexpression of carboxypeptidase Y (CPY) of Saccharomyces cerevisiae in Escherichia coli resulted in the formation of insoluble inclusion bodies. To produce soluble CPY we designed a novel Pichia pastoris expression system in which the following were inserted into expression vectors: three different signal sequences derived from the mating factor a1 of S. cerevisiae an inulinase of Kluyveromyces marxianus and the endogenous signal sequence of CPY. The expression vector pHIL-D2-SSinul-proCPY was the most effective in the production of proCPY among the vectors examined. The purified active CPY was obtained from proCPY by treating with proteinase K followed by QExcellose ion-exchange column chromatography.
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