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dc.contributor.authorHernández, J.G.
dc.contributor.authorArdila-Fierro, K.J.
dc.contributor.authorCrawford, Deborah E.
dc.contributor.authorJames, S.L.
dc.contributor.authorBolm, C.
dc.date.accessioned2020-03-03T15:24:12Z
dc.date.accessioned2020-03-09T15:40:11Z
dc.date.available2020-03-03T15:24:12Z
dc.date.available2020-03-09T15:40:11Z
dc.date.issued2017-05
dc.identifier.citationHernández JG, Ardila-Fierro KJ, Crawford DE et al (2017) Mechanoenzymatic peptide and amide bond formation. Green Chemistry. 19(11): 2620-2625.en_US
dc.identifier.urihttp://hdl.handle.net/10454/17698
dc.descriptionNoen_US
dc.description.abstractMechanochemical chemoenzymatic peptide and amide bond formation catalysed by papain was studied by ball milling. Despite the high-energy mixing experienced inside the ball mill, the biocatalyst proved stable and highly efficient to catalyse the formation of α,α- and α,β-dipeptides. This strategy was further extended to the enzymatic acylation of amines by milling, and to the mechanosynthesis of a derivative of the valuable dipeptide L-alanyl-L-glutamine.en_US
dc.description.sponsorshipWe thank RWTH Aachen University for support from the Distinguished Professorship Program funded by the Excellence Initiative of the German federal and state governments. EPSRC, grant no. EP/L019655/1.en_US
dc.language.isoenen_US
dc.subjectMechanochemical chemoenzymatic peptideen_US
dc.subjectAmide bond formationen_US
dc.subjectPapainen_US
dc.subjectBall millingen_US
dc.titleMechanoenzymatic peptide and amide bond formationen_US
dc.status.refereedYesen_US
dc.date.Accepted2017-04-28
dc.date.application2017-05-02
dc.typeArticleen_US
dc.type.versionNo full-text in the repositoryen_US
dc.identifier.doihttps://doi.org/10.1039/C7GC00615B
dc.date.updated2020-03-03T15:24:13Z


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