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BTI1, an azoreductase with pH-dependent substrate specificity.

ABSTRACT: The group II azoreductase BTI1 utilizes NADPH to directly cleave azo bonds in water-soluble azo dyes, including quenchers of fluorescence. Unexpectedly, optimal reduction was dye specific, ranging from a pH of <5.5 for Janus green B, to pH 6.0 for methyl red, methyl orange, and BHQ-10, to pH >8.3 for flame orange.

SUBMITTER: Johansson HE 

PROVIDER: S-EPMC3131635 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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BTI1, an azoreductase with pH-dependent substrate specificity.

Johansson Hans E HE   Johansson Mary K MK   Wong Albert C AC   Armstrong Eliana S ES   Peterson Erik J EJ   Grant Richard E RE   Roy Margaret A MA   Reddington Mark V MV   Cook Ronald M RM  

Applied and environmental microbiology 20110429 12

The group II azoreductase BTI1 utilizes NADPH to directly cleave azo bonds in water-soluble azo dyes, including quenchers of fluorescence. Unexpectedly, optimal reduction was dye specific, ranging from a pH of <5.5 for Janus green B, to pH 6.0 for methyl red, methyl orange, and BHQ-10, to pH >8.3 for flame orange. ...[more]

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