Earticle

초록

영어

There are several pathways for secreting proteins in periplasm. Among them, twin arginine translocation (Tat) pathway express protein in periplasm after it is folded in cytoplasm. When organophosphorus hydrolase (OPH) is expressed with Tat signal sequence in Escherichia coli, inclusion body in cytoplasm is a major form. This can cause a possibility of low whole cell activity. In the present work, we investigated a strategy for overcoming this problem in a whole cell system by enforcing periplasmic secretion of OPH through chaperone co-expression. We co-expressed molecular chaperone including GroEL/ES with OPH. We found significant increase of OPH in a soluble form compared to that without chaperone and this might be due to increased protein folding. Furthermore, whole cell OPH activity of chaperone co-expressing cells was about 20 times greater than that of non-expressing cells. Consequently, whole cell activity can be enhanced by chaperone co-expression.

키워드

저자

• Im Gyu KIM [ Dept. of Chemical Engineering, Pohang University of Science and Technology,Pohang,790-784. ]
• Dong Gyun KANG [ Dept. of Chemical Engineering, Pohang University of Science and Technology,Pohang,790-784. ]
• Hyung Joon CHA [ Dept. of Chemical Engineering, Pohang University of Science and Technology,Pohang,790-784. ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576