DUGiDocsInducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution
dc.contributor.author
dc.date.accessioned
2019-04-23T09:13:42Z
dc.date.available
2019-04-23T09:13:42Z
dc.date.issued
2017-01-01
dc.identifier.issn
1359-7345
dc.identifier.uri
dc.description.abstract
The long-standing problem of achieving high activity of a thermophilic enzyme at low temperatures and short reaction times with little tradeoff in thermostability has been solved by directed evolution, an alcohol dehydrogenase found in hot springs serving as the catalyst in enantioselective ketone reductions
dc.format.mimetype
application/pdf
dc.language.iso
eng
dc.publisher
The Royal Society of Chemistry
dc.relation.isformatof
Reproducció digital del document publicat a: https://doi.org/10.1039/C7CC05377K
dc.relation.ispartof
Chemical Communications, 2017, vol. 53, p. 9454-9457
dc.relation.ispartofseries
Articles publicats (D-Q)
dc.rights
Attribution 4.0 International
dc.rights.uri
dc.subject
dc.title
Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution
dc.type
info:eu-repo/semantics/article
dc.rights.accessRights
info:eu-repo/semantics/openAccess
dc.type.version
info:eu-repo/semantics/publishedVersion
dc.identifier.doi
dc.identifier.idgrec
027503
dc.type.peerreviewed
peer-reviewed
dc.identifier.eissn
1364-548X