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Updated: Jul 10, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Characterization and some reaction-engineering aspects of thermostable extracellular beta-galactosidase from a new
R K Sani1, S Chakraborti, R C Sobti
1Institute of Microbial Technology, Chandigarh, India.
Abstract:
A new strain of Bacillus sp. was isolated from a hot water spring in India. This strain generated a high activity of extracellular beta-galactosidase at 37 degrees C in shake flasks. The beta-galactosidase activity was found to increase continuously but the production rate was slower than with some other organisms reported in the literature. There were noteworthy differences in the time-domain profiles of bacterial concentration and beta-galactosidase activity when the starting concentration of substrate (glucose) was tripled from 10 g/L. These differences may be explained in terms of the relative rates of enzyme synthesis and its diffusion across the cell wall. The enzyme produced by this organism is more stable than other beta-galactosidases; its half-life is 408 h at 50 degrees C and 94 h at 55 degrees C, while the reported enzymes showed perceptible loss of activity within 2 h.
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