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Carbonyl
reductase of Candida parapsilosis CPCR
 The
NADH-dependent carbonyl reductase from Candida parapsilosis CPCR has
been successfully overexpressed in E.coli and the expression
level has reached about 30% of the total bacteria protein.
The CPCR shows a high enantioselectivity and a very broad substrate
range: aliphatic, cyclic and aromatic ketones, diketones and keto
acid esters, different compounds can be converted in high
enantiomeric purity e.g. S-2-Butanol.
Important
properties concerning the application of the enzyme are the
relatively broad pH optimum between pH 6.5 and 9.0, temperature
optimum between 36 and 42 degrees C, and good stability.
The
carbonyl reductase from C. parapsilosis is a dimeric enzyme
with an apparent molecular mass of about 135 kDa. This biocatalyst
offers the possibility for production purposes of enantiomerically
pure alcohols with S-Configuration. Methyl 3-oxobutanoate was
converted into methyl (S)-(+)-3- hydroxybutanoate (98.5% ee)
X-Zyme
Biotechnology also provides access to unique libraries of
oxidoreductases variants and conducts the screening of these
libraries for the selection of biocatalysts with desired properties.
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