Characteristics of a newly isolated fungus, Geotrichum candidum Dec 1, which decolorizes various dyes

Kim, Seong Jun; Ishikawa, Keisuke; Hirai, Mitsuyo; Shoda, Makoto

doi:10.1016/0922-338x(95)94755-g

Cited by 127 publications

(84 citation statements)

References 17 publications

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“…The newly isolated Geotrichum candidum Dec 1 was found to decolorize 21 kinds of synthetic dyes (13), and its degradation spectrum in relation to synthetic dyes is wider than that of any other decolorizing organisms reported so far. In our previous study, an extracellular enzyme, DyP (for dye-decolorizing peroxidase), was found to be responsible for the decolorization of dyes.…”

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confidence: 99%

Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

Sugano

Nakano

Sasaki

et al. 2000

Appl Environ Microbiol

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Efficient expression of the dye-decolorizing peroxidase, DyP, from Geotrichum candidum Dec 1 in Aspergillus oryzae M-2-3 was achieved by fusing mature cDNA encoding dyp with the A. oryzae ␣-amylase promoter (amyB). The activity yield of the purified recombinant DyP (rDyP) was 42-fold compared with that of the purified native DyP from Dec 1. No exogenous heme was necessary for the expression of rDyP in A. oryzae. From the N-terminal amino acid sequence analyses of native DyP and rDyP, the absence of a histidine residue in both DyPs, which was considered to be important for heme binding of DyP, was confirmed. These results suggest that rDyP without a typical heme-binding region produced by A. oryzae exhibits a function similar to that of native DyP.The newly isolated Geotrichum candidum Dec 1 was found to decolorize 21 kinds of synthetic dyes (13), and its degradation spectrum in relation to synthetic dyes is wider than that of any other decolorizing organisms reported so far. In our previous study, an extracellular enzyme, DyP (for dye-decolorizing peroxidase), was found to be responsible for the decolorization of dyes. DyP degraded phenolic compounds, such as 2,6-dimethoxyphenol and guaiacol, while it did not degrade nonphenolic veratryl alcohol (14). Considering its substrate specificity and molecular mass, DyP was found to be a novel peroxidase distinct from other peroxidases reported previously (25,26,28,41). Furthermore, the absorption spectrum of DyP exhibited a Soret band at 406 nm corresponding to a hemoprotein, and its Na 2 S 2 O 4 -reduced form revealed a peak at 556 nm that indicates the presence of a protoheme as its prosthetic group (14). We also reported the cloning of cDNA of the dyp gene (32).So far, several microorganisms capable of decolorizing some synthetic dyes have been reported (17-20, 22, 23). In particular, the white-rot fungus Phanerochaete chrysosporium was extensively studied as a dye-decolorizing fungus (5,9,19,20,21,30) and several lignin peroxidases (LiPs) of P. chrysosporium have been reported to show decolorizing activity. However, their decolorizing spectrum toward dyes is not extensively investigated, mainly because research on their lignin-degrading reaction is focused. Furthermore, although cloning and expression of several LiPs have been reported (6,11,29), there is no report on the enhancement of the yield of these enzymes by heterologous expression.Therefore, we focused on producing a large amount of DyP having dye-decolorizing activity in Aspergillus oryzae under the control of the amyB promoter. A. oryzae is known to exhibit a high growth rate and to be a safe host (1); furthermore, it can secrete gram-per-liter quantities of heterologous protein (4). From this study and our previous data, we show that DyP is a unique peroxidase.Chemicals, enzymes, and other materials. Ten kinds of synthetic dyes kindly provided by Nippon Kayaku Co., Ltd. (Tokyo, Japan), and Bayer Japan Co., Ltd. (Tokyo, Japan), were used. Cellulase and lysing enzymes were obtained from SigmaAldrich Japan...

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confidence: 99%

Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

Sugano

Nakano

Sasaki

et al. 2000

Appl Environ Microbiol

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“…The groups DyPA-C comprise predominantly bacterial enzymes, whereas DyPD is a fungal group (6). The first DyP was discovered in 1995 (7). A mixture of extracellular enzymes secreted by the basidiomycete Bjerkandera adusta (the strain was back then misidentified as Thanatephorus cucumeris) was reported to efficiently oxidize anthraquinone dyes such as Reactive Blue 5 (7,8).…”

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“…The first DyP was discovered in 1995 (7). A mixture of extracellular enzymes secreted by the basidiomycete Bjerkandera adusta (the strain was back then misidentified as Thanatephorus cucumeris) was reported to efficiently oxidize anthraquinone dyes such as Reactive Blue 5 (7,8). The enzyme responsible for the decolorization process was characterized as a heme peroxidase of unusual chemical properties.…”

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First Crystal Structure of a Fungal High-redox Potential Dye-decolorizing Peroxidase

Strittmatter

Liers

Ullrich

et al. 2013

Journal of Biological Chemistry

116

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Background: DyP-type peroxidases catalyze biotechnologically important reactions. Results: Based on the crystal structure of a fungal DyP, the conformational flexibility of Asp-168 is elucidated. Tyr-337 is identified as a surface-exposed substrate interaction site. Conclusion: Asp-168 and Tyr-337 are key residues directly involved in AauDyPI-catalysis. Significance: Peroxidases are biocatalysts, much sought after and ubiquitous enzymes in nature.

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“…Enzymes such as lignin peroxidase (LiP), manganese-dependent peroxidase (MnP) and laccase, all of which are involved in lignin degradation, have been reported to decolourize the synthetic dyes [28]. Kim et al [66] demonstrated the presence of H 2 O 2 dependent enzyme activity to declourize the dye Brilliant Blue R by the fungus Pleurotus ostreatus. Buswell et al [67] reported that the production of the extracellular ligninolytic enzymes is strongly affected by the nature and amount of the nutrients, especially nitrogen (N) and microelements, in the growth substrate.…”

Section: Mechanism Of Dye Degradationmentioning

confidence: 99%

Biodegradation of Synthetic Dyes: A Mycoremediation Approach for Degradation/Decolourization of Textile Dyes and Effluents

Singh

2017

JABB

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Present review highlights the role of fungi in biodegradation/decolourization of textile dyes and effluents. Though, fungi and bacteria both are the principal decomposer of xenobiotics in the environment but fungi are superior to bacteria in dyes degradation/decolourization due to their superiority in the production of dyes degrading enzymes and as absorbent. The present study focused on the achievements and advancement on the fungal degradation/decolourization of textiles dyes and effluents by the application of potent fungal strains. The biodegradation through fungi or myco-remediation of textile dyes and effluents using potential fungi is comparatively cheap and environmentally safe process, to decompose or mineralize the hardly or less degrading compounds of synthetic dyes. Fungi play an important role to degrade/decolourize the synthetic dyes through enzymes as well as by the absorption, adsorption and accumulation of colourants from the effluents.

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Characteristics of a newly isolated fungus, Geotrichum candidum Dec 1, which decolorizes various dyes

Cited by 127 publications

References 17 publications

Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

First Crystal Structure of a Fungal High-redox Potential Dye-decolorizing Peroxidase

Biodegradation of Synthetic Dyes: A Mycoremediation Approach for Degradation/Decolourization of Textile Dyes and Effluents

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