Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 5

The DOI matches its Crossref record, with a small difference in title or year; 170 of the 170 references it cites were found in a registry or an index.

Explorations and Applications of Enzyme-linked Bioremediation of Synthetic Dyes

Ogola, Henry Joseph Oduor, Ashida, Hiroyuki, Ishikawa, Takahiro, Sawa, Yoshihiro·2015·Advances in Bioremediation of Wastewater and Polluted Soil
DOI 10.5772/60753
Open this paper in CoChat — free account

Abstract

Extensive use of synthetic dyes and their subsequent release in industrial wastewater is a growing environmental problem. These dyes are recalcitrant in nature, and some dyes are also well established to be potentially carcinogenic and mutagenic as well as genotoxic. Research efforts have been devoted to develop new, low-cost, and eco-friendly treatments capable of reducing and even eliminating synthetic dye compounds from the environment. Enzymatic approach has attracted much interest recently in the decolorization of textile and other industrially important dyes from wastewater as an alternative strategy to conventional chemical, physical, and biological treatments, which pose serious limitations. In this chapter, the accumulated research data on the potential of the oxidoreductive enzymes—high redox potential peroxidases (lignin peroxidase [LiP], EC 1.11.1.14; manganese peroxidase [MnP], EC 1.11.1.13; dye decolorizing peroxidase [DyP], EC 1.11.1.19; and versatile peroxidases [VP], EC 1.11.1.16), laccases (benzenediol–oxygen oxidoreductase, EC 1.10.3.2), polyphenol oxidases (EC 1.14.18.1), and azoreductases (azobenzene reductases, EC 1.7.1.6)—that have been exploited in the decolorization and degradation of synthetic dyes are presented. An overview of enzyme technology, including the importance of redox mediators for enhanced range of substrates and efficiency of degradation, current biodegradation applications, and suggestions to overcome the limitations to these proteins’ large scale and efficient use, is made. Different strategies currently being used and future prospects for the potential use of genetic engineering techniques to improve the performance of these oxidoreductases in terms of stability, selectivity, and catalytic activity in dye bioremediation technologies are also explored.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.5772/60753

Cites

170 of 170 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1 Chemical structure of major synthetic dye compounds showing their chromophoric groups (in red) and different auxochromes.
Figure 1 Chemical structure of major synthetic dye compounds showing their chromophoric groups (in red) and different auxochromes.CC-BY · From the PDF
Figure 2 The structural model of DyP showing the heme active site architecture. (a) Typical α+β protein structure of DyP and the heme active site showing the conservation of key catalytic proximal Fe-His-Asp triad residues and substitution of His with Asp in the distal heme active. (b) Possible coordination of distal Asp and other active site residues with a water molecule involving hydrogen-bond network in the heme active site as implicated by the resolved crystal structures of ferric DyP enzymes [82-84].
Figure 2 The structural model of DyP showing the heme active site architecture. (a) Typical α+β protein structure of DyP and the heme active site showing the conservation of key catalytic proximal Fe-His-Asp triad residues and substitution of His with Asp in the distal heme active. (b) Possible coordination of distal Asp and other active site residues with a water molecule involving hydrogen-bond network in the heme active site as implicated by the resolved crystal structures of ferric DyP enzymes [82-84].CC-BY · From the PDF
Figure 3 Decolorization of azo dyes in the presence of mediators by AnaPX. (a) Biotransformation of Reactive Black 5 by AnaPX in the presence of various mediators. Inset shows the structures of the mediators and the resultant product upon decolorization. (b) Decolorization profile of several azo dyes by AnaPX in presence of different mediator. compounds.
Figure 3 Decolorization of azo dyes in the presence of mediators by AnaPX. (a) Biotransformation of Reactive Black 5 by AnaPX in the presence of various mediators. Inset shows the structures of the mediators and the resultant product upon decolorization. (b) Decolorization profile of several azo dyes by AnaPX in presence of different mediator. compounds.CC-BY · From the PDF
Figure 4 Biotransformation of AQ dye Reactive Blue 5 by AnaPX. The formation of characteristic light reddish brown product (2,2-disulfonyl azobenzene) upon enzymatic degradation of (a) Reactive Blue 5 and (c) other AQ dyes, Reactive Blue 4, Reactive Blue 19, and Reactive Blue 114. (b) UV absorption spectra of the degradation process showing the decrease in absorbance at 600 nm and an increase in absorbance at 400-500 nm. Each spectrum was taken after 4-s intervals.
Figure 4 Biotransformation of AQ dye Reactive Blue 5 by AnaPX. The formation of characteristic light reddish brown product (2,2-disulfonyl azobenzene) upon enzymatic degradation of (a) Reactive Blue 5 and (c) other AQ dyes, Reactive Blue 4, Reactive Blue 19, and Reactive Blue 114. (b) UV absorption spectra of the degradation process showing the decrease in absorbance at 600 nm and an increase in absorbance at 400-500 nm. Each spectrum was taken after 4-s intervals.CC-BY · From the PDF
Figure 5 (a) H 2 O2 stability of wild-type AnaPX and Met-substituted variants. (b) Dye decolorization activity of AnaPX and two improved variants (M401F and M451I) on AQ and azo dyes at two different H 2 O2 concentrations (1 and 5 mM) [80].
Figure 5 (a) H 2 O2 stability of wild-type AnaPX and Met-substituted variants. (b) Dye decolorization activity of AnaPX and two improved variants (M401F and M451I) on AQ and azo dyes at two different H 2 O2 concentrations (1 and 5 mM) [80].CC-BY · From the PDF

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 5

  1. Jadhav, J.P., et al., Decoloration of textile dyes by Trametes versicolor and its effect on dye toxicity. Biotechnology Letters, 2002. 24(21):1757-1761.
  2. Dunford, H.B. and H.B. Dunford, Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology, and Physiology. 2nd ed. 2010, Hoboken, NJ: John Wiley & Sons. xv, 459 pp.
  3. Strittmatter, E., D.A. Plattner, and K. Piontek, Dye-Decolorizing Peroxidase (DyP), in Encyclopedia of Inorganic and Bioinorganic Chemistry. 2011, John Wiley & Sons, Ltd.
  4. Xu, F., Laccase, in Encyclopedia of Bioprocess Technology. 2002, John Wiley & Sons, Inc.
  5. Nachiyar, C.V. and G.S. Rajkumar, Degradation of a tannery and textile dye, Navitan Fast Blue S5R by Pseudomonas aeruginosa. World Journal of Microbiology and Biotechnolo- gy, 2003. 19(6):609-614.

Cited by

See all 5

Metadata

Authors
Ogola, H. J. O., Ashida, H., Ishikawa, T., & Sawa, Y.
Venue
Advances in Bioremediation of Wastewater and Polluted Soil
Publisher
InTech
Published
2015-09-09
DOI
10.5772/60753
Cited by
5
References
170
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.