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Literature summary for 1.2.1.3 extracted from

  • Sankaranarayanan, M.; Seol, E.; Kim, Y.; Chauhan, A.S.; Park, S.
    Measurement of crude-cell-extract glycerol dehydratase activity in recombinant Escherichia coli using coupled-enzyme reactions (2017), J. Ind. Microbiol. Biotechnol., 44, 477-488 .
    View publication on PubMed

Application

Application Comment Organism
analysis a reliable, enzyme-coupled assay for measuring glycerol dehydratase activity in crude-cell extract is developed using 1,2-propanediol as the substrate. In the assay, 1,2-propanediol is converted to propionaldehyde, which is quickly converted to 1-propionic acid by aldehyde dehydrogenase (with the production of NADH) or to 1-propanol by yeast alcohol dehydrogenase (with the consumption of NADH). The change in NADH concentration, as monitored at 340 nm spectrophotometrically, manifested as a straight line for 3 min, from which the glycerol dehydratase activity can be determined. Cells are assumed to have been disintegrated by physical methods (Bead Beater or French Press), not by chemical methods. The assay method should prove to be applicable to recombinant strains developed for the production of 3-hydroxypropionic acid and/or and/or 1,3-propanediol from glycerol Azospirillum brasilense

Organism

Organism UniProt Comment Textmining
Azospirillum brasilense
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Synonyms

Synonyms Comment Organism
ALDH
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Azospirillum brasilense
KGSADH
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Azospirillum brasilense