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Covalently immobilized Trp60Cys mutant of omega‰-transaminase from Chromobacterium violaceum for kinetic resolution of racemic amines in batch and continuous-flow modes
Vise andre og tillknytning
2018 (engelsk)Inngår i: Biochemical engineering journal, ISSN 1369-703X, E-ISSN 1873-295X, Vol. 132, s. 270-278Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Covalent immobilization of an engineered omega-transaminase mutant Trp60Cys from Chromobacterium violaceum (CvTAW60C) was performed on bisepoxide-activated aminoalkyl resins. Activity of the various CvTAW60C preparations was evaluated in kinetic resolution of four racemic amines (rac-1a–d). The most active EA-G-CvTAW60C preparation (CvTAW60C attached to polymeric resin with ethylamine function activated with glycerol diglycidyl ether—EA-G) could perform the kinetic resolution of racemic 4-phenylbutan-2-amine (rac-1a) over 49% conversion up to 19 consecutive reaction cycles or in media containing up to 50% v/v DMSO as cosolvent in batch mode reactions. The immobilization process of CvTAW60C onto the EA-G resin filled in stainless steel bioreactors was also tested in flow-through mode. Kinetic resolution of three racemic amines containing aromatic moieties (rac-1a-c) was performed in continuous-flow mode resulting in easy-to-separate mixture of the corresponding ketone (2a–c) and the non-converted (R)-amine in high enantiopurity (ee(R)-1a-c ≥ 96%).

sted, utgiver, år, opplag, sider
Elsevier, 2018. Vol. 132, s. 270-278
Emneord [en]
Transaminase, Covalent immobilization, Amine, Kinetic resolution, Continuous-flow biocatalysis
HSV kategori
Forskningsprogram
Bioteknologi
Identifikatorer
URN: urn:nbn:se:kth:diva-224456DOI: 10.1016/j.bej.2018.01.022ISI: 000433266500030Scopus ID: 2-s2.0-85041399379OAI: oai:DiVA.org:kth-224456DiVA, id: diva2:1191336
Merknad

QC 20180326

Tilgjengelig fra: 2018-03-18 Laget: 2018-03-18 Sist oppdatert: 2018-06-25bibliografisk kontrollert

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Land, HenrikBerglund, Per
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