Biochemical characterization of a novel azo reductase named BVU5 from the bacterial flora DDMZ1: application for decolorization of azo dyes.
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ABSTRACT: One of the main mechanisms of bacterial decolorization and degradation of azo dyes is the use of biological enzymes to catalyze the breaking of azo bonds. This paper shows the expression and properties of a novel azo reductase (hybrid-cluster NAD(P)-dependent oxidoreductase, accession no. A0A1S1BVU5, named BVU5) from the bacterial flora DDMZ1 for degradation of azo dyes. The molecular weight of BVU5 is about 40.1 kDa, and it contains the prosthetic group flavin mononucleotide (FMN). It has the decolorization ability of 80.1 ± 2.5% within 3 min for a dye concentration of 20 mg L-1, and 53.5 ± 1.8% even for a dye concentration of 200 mg L-1 after 30 min. The optimum temperature of enzyme BVU5 is 30 °C and the optimum pH is 6. It is insensitive to salt concentration up t
SUBMITTER: Cong J
PROVIDER: S-EPMC8979046 | biostudies-literature | 2022 Jan
REPOSITORIES: biostudies-literature
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