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Reductive biotransformations of organic compounds by saccharomyces cerevisiae: Study of oxidoreductases involved using electrophoretic zymograms
Author(s) -
Young C. S.,
Ward O. P.
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260390413
Subject(s) - nad+ kinase , nicotinamide adenine dinucleotide , cofactor , nicotinamide , chemistry , biochemistry , enzyme , zymography , stereochemistry , chromatography
The role of oxidoreductases in reduction of carbonyl compounds was investigated by application of zymogram techniques. Eight bands were observed using ethanol with nicotinamide adenine dinucleotide (NAD) as coenzyme. Bands observed with lactic acid and (R)‐(‐)‐phenyl‐1,2‐ethanediol with nicotinamide adenine dinucleotide phosphate (NADP) had similar R m values. 2‐Hydroxyvalerate and malate manifested bands having similar R m values and were active with both NAD and NADP. Based on their structural similarity and identical R m values, oxidation of 1,4‐cyclooctanediol (band #2) and cis ‐1,5‐cyclooctanediol may be due to a common enzyme. The PAGE‐zymogram technique may be used on a preparative scale to facilitate purification and full characterization on the observed stained bands.