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Published September 2001 | public
Journal Article

Expression and stabilization of galactose oxidase in Escherichia coli by directed evolution

Abstract

We have used directed evolution methods to express a fungal enzyme, galactose oxidase (GOase), in functional form in Escherichia coli. The evolved enzymes retain the activity and substrate specificity of the native fungal oxidase, but are more thermostable, are expressed at a much higher level (up to 10.8 mg/l of purified GOase), and have reduced negative charge compared to wild type, all properties which are expected to facilitate applications and further evolution of the enzyme. Spectroscopic characterization of the recombinant enzymes reveals a tyrosyl radical of comparable stability to the native GOase from Fusarium.

Additional Information

© 2001 Oxford University Press. Received January 30, 2001. Accepted May 15, 2001. This work was supported by the Biotechnology Research and Development Corporation.

Additional details

Created:
August 19, 2023
Modified:
October 24, 2023