Functional display of foreign protein on surface of Escherichia coli using N-terminal domain of ice nucleation protein
β Scribed by Lin Li; Dong Gyun Kang; Hyung Joon Cha
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 550 KB
- Volume
- 85
- Category
- Article
- ISSN
- 0006-3592
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A surface anchoring motif using the ice nucleation protein (INP) of Xanthomonas campestris pv. campestris BCRC 12846 for display of transglucosidase has been developed. The transglucosidase gene from Xanthomonas campestris pv. campestris BCRC 12608 was fused to the truncated ina gene. This truncated
## Abstract Methyl parathion hydrolase (MPH) has been displayed on the surface of microorganisms for the first time using only Nβ and Cβterminal domains of the ice nucleation protein (INPNC) from __Pseudomonas syringae__ INA5 as an anchoring motif. A shuttle vector pINCM coding for INPNCβMPH was co