Journal
BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
Volume 17, Issue 4, Pages 687-692Publisher
KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
DOI: 10.1007/s12257-012-0093-3
Keywords
Candida antarctica lipase B; soluble expression; fusion protein; Skp
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Funding
- National Research Foundation of Korea
- Korean Government (MEST) [NRF-2009-C1AAA001-2009-0093512]
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Candida antarctica lipase B (CalB) is an industrially versatile enzyme, especially for biodiesel production and organic synthesis. Recombinant expression using the E. coli system has advantages, such as lower costs, easier handling, and higher number of clones that can be screened daily compared to expression using higher organism. But the expression of CalB in E. coli is not feasible because insoluble aggregates are formed and proteolytic degradation is known to occur during expression. In this study, fusion proteins were designed to express soluble CalB in E. coli. The periplasmic chaperone of E. coli, Skp was fused with CalB and this fusion protein showed a high solubility (yielding 82.5 mu g/mL). The fusion protein system can be applied to the rapid expression and evaluation of CalB variants for functional improvement.
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