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dc.contributor.authorAlami, Ayoub Talbi
dc.contributor.authorRichina, Frederica
dc.contributor.authorHernandez, Maria
dc.contributor.authorDudal, Yves
dc.contributor.authorShahgaldian, Patrick
dc.date.accessioned2018-12-13T09:57:44Z
dc.date.available2018-12-13T09:57:44Z
dc.date.issued2018-05
dc.identifier.issn2673-2424
dc.identifier.issn0009-4293
dc.identifier.doi10.2533/chimia.2017.345
dc.identifier.urihttp://hdl.handle.net/11654/26975
dc.description.abstractTransaminases are enzymes capable of stereoselective reductive amination; they are of great interest in the production of chiral building blocks. However, the use of this class of enzymes in industrial processes is often hindered by their limited stability under operational conditions. Herein, we demonstrate that a transaminase enzyme from Aspergillus terreus can be immobilized at the surface of silica nanoparticles and protected in an organosilica shell of controlled thickness. The so-protected enzyme displays a high biocatalytic activity, and additionally provides the possibility to be retained in a reactor system for continuous operation and to be recycled.
dc.language.isoen
dc.publisherSchweizerische Chemische Gesellschaften_US
dc.relation.ispartofChimiaen_US
dc.accessRightsAnonymous
dc.subjectChiral building blocks
dc.subjectTransaminases
dc.titleSurface Immobilization and Shielding of a Transaminase Enzyme for the Stereoselective Synthesis of Pharmaceutically Relevant Building Blocks
dc.type01A - Beitrag in wissenschaftlicher Zeitschrift
dc.volume72
dc.issue5
dc.audienceScience
fhnw.publicationStatePublished
fhnw.ReviewTypeAnonymous ex ante peer review of a complete publication
fhnw.InventedHereYes
fhnw.PublishedSwitzerlandNo
fhnw.pagination345-346
fhnw.IsStudentsWorkno
fhnw.publicationOnlineJa


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