Stabilization of an amine transaminase for biocatalysis
2016 (English)In: Journal of Molecular Catalysis B: Enzymatic, ISSN 1381-1177, E-ISSN 1873-3158, Vol. 124, 20-28 p.Article in journal (Refereed) Published
The amine transaminase from Chromobacterium violaceum (Cv-ATA) is a well-known enzyme to achievechiral amines of high enantiomeric excess in laboratory scales. However, the low operational stabilityof Cv-ATA limits the enzyme applicability on larger scales. In order to improve the operational stabilityof Cv-ATA, and thereby extending its applicability, factors (additives, co-solvents, organic solvents anddifferent temperatures) targeting enzyme stability and activity were explored in order to find out how tostore and apply the enzyme. The present investigation shows that the melting point of Cv-ATA is improvedby adding sucrose or glycerol, separately. Further, by storing the enzyme at higher concentrations and inco-solvents, such as; 50% glycerol, 20% methanol or 10% DMSO, the active dimeric structure of Cv-ATAis retained. Enzyme stored in 50% glycerol at −20◦C was e.g., still fully active after 6 months. Finally,the enzyme performance was improved 5-fold by a co-lyophilization with surfactants prior to usage inisooctane.
Place, publisher, year, edition, pages
Elsevier, 2016. Vol. 124, 20-28 p.
Biocatalysis and Enzyme Technology
Research subject Biotechnology
IdentifiersURN: urn:nbn:se:kth:diva-180821DOI: 10.1016/j.molcatb.2015.11.022ISI: 000370458100003ScopusID: 2-s2.0-84949440870OAI: oai:DiVA.org:kth-180821DiVA: diva2:897101
QC 20160126. QC 201603192016-01-242016-01-242016-03-19Bibliographically approved