Dataset Information

Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator.

ABSTRACT: A multicopper oxidase (IOX) produced by Iodidimonas sp. Q-1 has high catalytic efficiency for iodide (I-) oxidation to form molecular iodine (I2). In this study, the potential capacity of IOX for decolorization of recalcitrant dyes was determined. Although IOX did not decolorize any dyes in the absence of redox mediator, significant decolorization of Orange G, Indigo Carmine, Amido Black, and Remazol Brilliant Blue R (RBBR) was observed in the presence of iodide. Addition of 0.1?mM iodide was sufficient to decolorize a total of 3?mM Indigo Carmine, suggesting that iodide functions as a mediator. Such mediator-like function of iodide was not observed in commercially available fungal laccases. The IOX-iodide decolorization system showed much alkaline pH optima of 5.5-6.5 and stronger salt tolerance than fungal laccases did. In addition, actual wastewater discharged from a dyeing factory could be decolorized more than 50% by the system. Since iodide is naturally occurring, non-toxic, and cheaper than common synthetic mediators, the IOX-iodide system is potentially more advantageous than fungal laccase-mediator systems for decolorization of recalcitrant dyes.

SUBMITTER: Taguchi T

PROVIDER: S-EPMC5928188 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator.

Taguchi Taro T Ebihara Kyota K Yanagisaki Chihiro C Yoshikawa Jun J Horiguchi Hirofumi H Amachi Seigo S

Scientific reports 20180430 1

A multicopper oxidase (IOX) produced by Iodidimonas sp. Q-1 has high catalytic efficiency for iodide (I<sup>-</sup>) oxidation to form molecular iodine (I<sub>2</sub>). In this study, the potential capacity of IOX for decolorization of recalcitrant dyes was determined. Although IOX did not decolorize any dyes in the absence of redox mediator, significant decolorization of Orange G, Indigo Carmine, Amido Black, and Remazol Brilliant Blue R (RBBR) was observed in the presence of iodide. Addition o ...[more]

PMID: 29712927

Similar Datasets

Project description:Multicopper oxidases (MCOs) are a family of enzymes that use copper ions as cofactors to oxidize various substrates. Previous research has demonstrated that several MCOs such as MnxG, MofA and MoxA can act as putative Mn(II) oxidases. Meanwhile, the endospore coat protein CotA from Bacillus species has been confirmed as a typical MCO. To study the relationship between CotA and the Mn(II) oxidation, the cotA gene from a highly active Mn(II)-oxidizing strain Bacillus pumilus WH4 was cloned and overexpressed in Escherichia coli strain M15. The purified CotA contained approximately four copper atoms per molecule and showed spectroscopic properties typical of blue copper oxidases. Importantly, apart from the laccase activities, the CotA also displayed substantial Mn(II)-oxidase activities both in liquid culture system and native polyacrylamide gel electrophoresis. The optimum Mn(II) oxidase activity was obtained at 53°C in HEPES buffer (pH 8.0) supplemented with 0.8 mM CuCl2. Besides, the addition of o-phenanthroline and EDTA both led to a complete suppression of Mn(II)-oxidizing activity. The specific activity of purified CotA towards Mn(II) was 0.27 U/mg. The Km, Vmax and kcat values towards Mn(II) were 14.85±1.17 mM, 3.01×10(-6)±0.21 M·min(-1) and 0.32±0.02 s(-1), respectively. Moreover, the Mn(II)-oxidizing activity of the recombinant E. coli strain M15-pQE-cotA was significantly increased when cultured both in Mn-containing K liquid medium and on agar plates. After 7-day liquid cultivation, M15-pQE-cotA resulted in 18.2% removal of Mn(II) from the medium. Furthermore, the biogenic Mn oxides were clearly observed on the cell surfaces of M15-pQE-cotA by scanning electron microscopy. To our knowledge, this is the first report that provides the direct observation of Mn(II) oxidation with the heterologously expressed protein CotA, Therefore, this novel finding not only establishes the foundation for in-depth study of Mn(II) oxidation mechanisms, but also offers a potential biocatalyst for Mn(II) removal.

Dataset Information

Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator.

Publications

Decolorization of recalcitrant dyes by a multicopper oxidase produced by Iodidimonas sp. Q-1 with iodide as a novel inorganic natural redox mediator.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets