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Compensatory stabilizing role of surface mutations during the directed evolution of dienelactone hydrolase for enhanced activity

Porter, Joanne L.; Collyer, Charles A.; Ollis, David L.


Directed evolution is a common tool employed to generate enzymes suitable for industrial use. High thermal stability is often advantageous or even a requirement for biocatalysts, as such the evolution of protein stability is of practical as well as academic interest. Even when evolving enzymes for new or improved catalytic functions, stability is an important factor since it can limit the accumulation rate and number of desired active site mutations. Dienelactone hydrolase, a small monomeric...[Show more]

CollectionsANU Research Publications
Date published: 2015-01-20
Type: Journal article
Source: The Protein Journal
DOI: 10.1007/s10930-015-9600-7


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