Journal
PROTEIN ENGINEERING
Volume 14, Issue 9, Pages 699-704Publisher
OXFORD UNIV PRESS
DOI: 10.1093/protein/14.9.699
Keywords
directed evolution; galactose oxidase; random mutagenesis; StEP recombination
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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/1 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.
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