Open AccessBTI1, an Azoreductase with pH-Dependent Substrate Specificity
Author(s) -
Hans Johansson,
Mary Katherine Johansson,
Albert C. Wong,
Eliana S. Armstrong,
Erik Peterson,
Richard E. Grant,
Margaret Roy,
Mark V. Reddington,
Ronald M. Cook
Publication year - 2011
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.02289-10
Subject(s) - cleave , orange (colour) , chemistry , fluorescence , methyl orange , orange g , photochemistry , janus , substrate (aquarium) , methyl red , nuclear chemistry , enzyme , biochemistry , food science , nanotechnology , materials science , catalysis , biology , optics , ecology , physics , photocatalysis
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 8.3 for flame orange.