## 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
β¦ LIBER β¦
Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae
β Scribed by Jung, Heung-Chae; Lebeault, Jean-Michel; Pan, Jae-Gu
- Book ID
- 109905204
- Publisher
- Nature Publishing Group
- Year
- 1998
- Tongue
- English
- Weight
- 757 KB
- Volume
- 16
- Category
- Article
- ISSN
- 1087-0156
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Surface display of MPH on Pseudomonas pu
β
Chao Yang; Ning Cai; Ming Dong; Hong Jiang; Jinming Li; Chuanling Qiao; Ashok Mu
π
Article
π
2007
π
John Wiley and Sons
π
English
β 186 KB
Surface display of transglucosidase on E
β
Po-Hung Wu; R. Giridhar; Wen-Teng Wu
π
Article
π
2006
π
John Wiley and Sons
π
English
β 227 KB
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