Development and characterization of membrane surface display system using molecular chaperon, prsA, of Bacillus subtilis
- Institute for Molecular Biology and Genetics, School of Chemical Engineering, Seoul National University, Seoul (Korea, Republic of)
We report a new membrane surface display system based on molecular chaperon, prsA, of Bacillus subtilis. Clostridium thermocellum cellulase, celA, was fused to C-terminal end of PrsA. Cellulase activity of B. subtilis protoplast, which expressed PrsA-CelA was 15 times higher compared to control strain. More than 85% of total cellulase activity was observed in surface displayed format and less than 15% of total cellulase activity was found in supernatant. Flow cytometric analysis of protoplast of PrsA-CelA fusion expressing bacteria provided another proof of uniform expression of fusion protein onto cytoplasmic membrane of B. subtilis. Without lysozyme treatment, only part of cellulase activity (10%) was observed in whole cell fraction.
- OSTI ID:
- 20710960
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 334, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2005.07.024; PII: S0006-291X(05)01488-9; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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