Earticle

초록

영어

Carboxypeptidase Y (CPY) is a useful enzyme involved in the amidation of therapeutic peptides and C-terminal sequencing of polypeptides. Endogenous CPY of Saccharomyces cerevisiae is initially expressed as a form of proCPY that contains the proregion and then is processed by vacuolar protease A for its conversion to the active form. CPY fused with the mating factor α (MFα) signal sequence was overexpressed under the control of the GAL1 promoter in recombinant S. cerevisiae. Batch fermentation of S. cerevisiae CENPK2-1D/p426αCPY resulted in 7.6 g/L dry cell mass and 14 mg/L CPY concentration. The mature form of CPY (61 kDa) and proCPY (67 kDa) were detected in the media. Pdi1p, an essential yeast protein catalyzing the oxidation, reduction, and isomerization of disulfide bond, was coexpressed at the same manner of CPY. Coexpression of Pdi1p enhanced the secretion of CPY. Finally, S. cerevisiae CENPK2-1D/p426αCPY+p424GalLPDI1 coexpressing CPY and Pdi1p produced 34 mg/L CPY, corresponding to a 2-fold increase compared with the control strain.

키워드

저자

• Wan NAM [ Dept. of Agricultural Biotechnology, Seoul National University, ]
• So-Yeon SHIN [ Dept. of Agricultural Biotechnology, Seoul National University, ]
• Seung-Ryul HAN [ Dept. of Agricultural Biotechnology, Seoul National University, ]
• Yu-Mi KIM [ Dept. of Agricultural Biotechnology, Seoul National University, ]
• Soo-Wan NAM [ Dept. of Biotechnology and Bioengineering, Dong-Eui University ]
• Yong-Cheol PARK [ Center for Agricultural Biomaterials, Seoul National University, ]
• Jin-Ho SEO [ Dept. of Agricultural Biotechnology, Seoul National University, ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576