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.
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