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Computational Thermostabilization of an Enzyme

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Science  06 May 2005:
Vol. 308, Issue 5723, pp. 857-860
DOI: 10.1126/science.1107387

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Abstract

Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10°C increase in apparent melting temperature Tm and a 30-fold increase in half-life at 50°C, with no reduction in catalytic efficiency. The effects of the mutations were synergistic, giving an increase in excess of the sum of their individual effects. The redesigned enzyme induced an increased, temperature-dependent bacterial growth rate under conditions that required its activity, thereby coupling molecular and metabolic engineering.

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