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dc.contributor.authorJahns, Anika C
dc.contributor.authorRehm, Bernd HA
dc.date.accessioned2017-07-28T02:54:52Z
dc.date.available2017-07-28T02:54:52Z
dc.date.issued2015
dc.identifier.issn0141-5492
dc.identifier.doi10.1007/s10529-014-1735-7
dc.identifier.urihttp://hdl.handle.net/10072/342769
dc.description.abstractPolyhydroxyalkanoate (PHA) beads, recombinantly produced in Escherichia coli, were functionalized to display lipase B from Candida antarctica as translational protein fusion. The respective beads were characterized in respect to protein content, functionality, long term storage capacity and re-usability. The direct fusion of the PHA synthase, PhaC, to lipase B yielded active PHA lipase beads capable of hydrolyzing glycerol tributyrate. Lipase B beads showed stable activity over several weeks and re-usability without loss of function.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherSpringer Netherlands
dc.relation.ispartofpagefrom831
dc.relation.ispartofpageto835
dc.relation.ispartofissue4
dc.relation.ispartofjournalBiotechnology Letters
dc.relation.ispartofvolume37
dc.subject.fieldofresearchEnvironmental Biotechnology not elsewhere classified
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchEngineering
dc.subject.fieldofresearchTechnology
dc.subject.fieldofresearchcode100299
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode09
dc.subject.fieldofresearchcode10
dc.titleImmobilization of active lipase B from Candida antarctica on the surface of polyhydroxyalkanoate inclusions
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorRehm, Bernd


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