The amino acid sequences of beta-glucosidases from Cellvibrio gilvus and Agrobacterium tumefaciens show significant similarity in most of the parts. However, the pH/temperature optima and stabilities of the two enzymes are quite different. C. gilvus beta-glucosidase exhibits an optimum pH of 6.2-6.4 and temperature of 35 degrees C, whereas the corresponding values for A. tumefaciens are 7.2-7.4 and 60 degrees C respectively. To analyse these properties further, a chimeric beta-glucosidase was constructed by replacing a segment from the C-terminal region of C. gilvus beta-glucosidase gene with that of A. tumefaciens. The partially purified chimeric enzyme was characterized with respect to pH/temperature activity and stability and substrate affinity. Our results suggest that C-terminal segment(s) might be important in beta-glucosidase specificity, and shuffling of even a small segment of gene in this region might significantly alter or improve the enzymic properties such as thermal stability.
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Research Article| February 01 1995
Construction and characterization of a chimeric β-glucosidase
T T Hoa;
Biochem J (1995) 305 (3): 715–719.
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A Singh, K Hayashi, T T Hoa, Y Kashiwagi, K Tokuyasu; Construction and characterization of a chimeric β-glucosidase. Biochem J 1 February 1995; 305 (3): 715–719. doi: https://doi.org/10.1042/bj3050715
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