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Chemija / Chemistry

ISSN 0235-7216
ISSN 2424-4538 (online)

2012 m. Nr. 3

Biocatalytic properties of quinohemoprotein alcohol dehydrogenase IIG from Pseudomonas putida HK5
Liucija MARCINKEVIČIENĖ, Jonita STANKEVIČIŪTĖ, Irina BACHMATOVA, Regina VIDŽIŪNAITĖ, Ana CHALECKAJA, Rolandas MEŠKYS

Quinohemoprotein alcohol dehydrogenases (ADHs) are attractive catalysts because of their wide substrate specificity and non-diffusible cofactor. ADH IIG from Pseudomonas putida HK5 is capable to oxidize various primary or secondary aliphatic and cyclic amino alcohols stereoselectively. An optimal pH range for ADH IIG activity has been shifted to more acidic side (pH 4–6) when amino alcohols were used as substrates. ADH IIG covalently immobilized on silica gel by cross-linking with glutaraldehyde or 1-ethyl-3(3-dimethylaminopropyl) carbodiimide exhibits a higher storage stability and thermostability as well as an improved activity in the presence of organic solvents comparing with the free enzyme. The affinity of ADH IIG to substrates has not been significantly changed in the presence of organic solvents or after the immobilization of the enzyme.

Keywords: alcohol dehydrogenase, pyrroloquinoline quinone, immobilization, organic solvents, enantioselective oxidation

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