XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

Posters
19.
PrODUCTION of TWO rECOMBINaNT aLCOHOLDEHYDrOGENaSES
SUITaBLE for BIOTraNSformaTION of C-6 aLDEHYDES INTO
COrESPONDING aLCOHOLS
Pavol Utekal, Lucia Pánčiová, Stanislav Stuchlík and Ján Turňa
Department of Molecular biology Prif UK Bratislava
C-6 aldehydes and alcohols contribute to the fresh green odor in plants and are widely
used in perfumes and in food technology. Important member of this family is trans-2-
hexenol. Carbonyl compounds such as aldehydes and alcohols are reduced by chemical
methods in industry but it is not appropriate for production of compounds used in
food industry. Therefore, in recent decades biocatalysis is used for these purposes. The
enzymes suitable for reduction of aldehydes are oxidoreductases, which catalyze the
reduction of carbonyl groups of aldehydes and alcohols. The most suitable enzyme from
this class is alcoholdehydrogenase (ADH), which is the last enzyme involved in lipoxygenase
pathway in several species of higher plants, which converts natural trans-2-hexenal
to trans-2-hexenol. In the case of redox reactions catalyzed by oxidoreductases, which
often require stoichiometric oxidation or reduction of costly coenzymes such as NAD(P)
and FAD, efficient coenzyme recycling must be accomplished if a given application is to
be practical from an economic standpoint. Formate dehydrogenase (FDH) is one of the
frequently used biocatalysts for NADH regeneration. This work is focused on the cloning,
expression, purification and measurements of enzyme activity of two enzymes - ADH
from Saccharomyces cerevisiae and FDH from Candida boidinii.
134 XXII. Biochemistry Congress, Martin