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• W1965621815 abstract "Chitinase from Bacillus thuringiensis and Bacillus licheniformis consisting of an N-terminal catalytic domain (GH18) and a C-terminal chitin-binding domain (ChBD), were cloned and characterised. In order to study the importance of individual domains, chimeric chitinases (BtGH-BliChBD and BliGH-BtChBD) were constructed using domain swapping as a strategy to exchange the CBD of BtGH-ChBD with that of BliGH-ChBD and vice versa. Both chimeric chitinases showed increased affinity to colloidal chitin. BtGH-BliChBD was different from the three other chitinases studied concerning optimum temperature and pH. Additionally, BtGH-BliChBD and BliGH-BtChBD showed significant improvement in functional stability, conformational stability, and binding ability towards insoluble chitinous substrates compared to those of the native chitinases." @default.
• W1965621815 created "2016-06-24" @default.
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• W1965621815 date "2010-01-01" @default.
• W1965621815 modified "2023-09-27" @default.
• W1965621815 title "Swapping the chitin-binding domain in Bacillus chitinases improves the substrate binding affinity and conformational stability" @default.
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• W1965621815 doi "https://doi.org/10.1039/b923048c" @default.
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