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- W2006385513 abstract "The amine transaminase from Chromobacterium violaceum (Cv-ATA) is a well-known enzyme to achieve chiral amines of high enantiomeric excess in laboratory scales. However, the low operational stability of Cv-ATA limits the enzyme applicability on larger scales. In order to improve the operational stability of Cv-ATA, and thereby extending its applicability, factors (additives, co-solvents, organic solvents and different temperatures) targeting enzyme stability and activity were explored in order to find out how to store and apply the enzyme. The present investigation shows that the melting point of Cv-ATA is improved by adding sucrose or glycerol, separately. Further, by storing the enzyme at higher concentrations and in co-solvents, such as; 50% glycerol, 20% methanol or 10% DMSO, the active dimeric structure of Cv-ATA is 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 in isooctane." @default.
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- W2006385513 date "2009-09-01" @default.
- W2006385513 modified "2023-10-16" @default.
- W2006385513 title "Suppression of water as a nucleophile in Pseudozyma (Candida) antarctica lipase B catalysis" @default.
- W2006385513 doi "https://doi.org/10.1016/j.nbt.2009.06.431" @default.
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