Decolorization of molasses and a dye by a newly isolated strain of the fungusGeotrichum candidum Dec 1

Kim, Seong Jun; Shoda, Makoto

doi:10.1002/(sici)1097-0290(19990105)62:1<114::aid-bit13>3.0.co;2-t

Cited by 64 publications

(22 citation statements)

References 11 publications

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“…The first indication of the existence of this peroxidase type was discovered by Kim et al ( 1995 ). The first enzyme of this family (Bad DyP) was extracted from the fungus Bjerkandera adusta and was consequently purified and characterized (Kim and Shoda 1999a ). In the meantime DyP-type peroxidases have not only been discovered in Basidiomycota, but also in Ascomycetes and bacteria (Hofrichter et al 2010 ).…”

Section: Introductionmentioning

confidence: 99%

Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus

et al. 2017

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The coding sequence of a peroxidase from the secretome of Pleurotus sapidus was cloned from a cDNA library. Bioinformatic analyses revealed an open reading frame of 1551 bp corresponding to a primary translation product of 516 amino acids. The DyP-type peroxidase was heterologously produced in Trichoderma reesei with an activity of 55,000 U L−1. The enzyme was purified from the culture supernatant, biochemically characterized and the kinetic parameters were determined. The enzyme has an N-terminal signal peptide composed of 62 amino acids. Analysis by Blue Native PAGE and activity staining with ABTS, as well as gel filtration chromatography showed the native dimeric state of the enzyme (115 kDa). Analysis of the substrate range revealed that the recombinant enzyme catalyzes, in addition to the conversion of some classic peroxidase substrates such as 2,2′-azino-bis(3-ethylthiazoline-6-sulfonate) and substituted phenols like 2,6–dimethoxyphenol, also the decolorization of the anthraquinonic dye Reactive Blue 5. The enzyme also catalyzes bleaching of natural colorants such as β-carotene and annatto. Surprisingly, β-carotene was transformed in the presence and absence of H2O2 by rPsaDyP, however enzyme activity was increased by the addition of H2O2. This indicates that the rPsaDyP has an oxidase function in addition to a peroxidase activity. As a consequence of the high affinity to the characteristic substrate Reactive Blue 5 the rPsaDyP belongs functionally to the dyp-type peroxidase family.

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Section: Introductionmentioning

confidence: 99%

Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus

et al. 2017

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“…A basidiomycete, Thanatephorus cucumeris Dec 1 (formerly called Geotrichum candidum Dec 1), isolated from soil, shows broad degrading activity toward poorly biodegradable materials such as lignin, molasses and synthetic dyes (Kim et al, 1995;Kim & Shoda, 1998, 1999aShintani et al, 2002). This fungus has potential for removing these wastes as an energy-saving treatment method.…”

Section: Introductionmentioning

confidence: 99%

A unique dye-decolorizing peroxidase, DyP, fromThanatephorus cucumerisDec 1: heterologous expression, crystallization and preliminary X-ray analysis

Sato

Hara

Matsui

et al. 2003

Acta Crystallogr D Biol Cryst

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The dye-decolorizing peroxidase DyP is a key enzyme in the decolorizing fungus Thanatephorus cucumeris Dec 1 that degrades azo and antraquinone dyes. The gene dyp from T. cucumeris Dec 1, which has low homology to other peroxidase genes, was cloned and transformed into Aspergillus oryzae and glycosylated DyP was expressed at high levels. Puri®ed DyP was deglycosylated using GST Endo F1 and then crystallized in a strong magnetic ®eld (10 T) at 283 K using ammonium sulfate as precipitant. X-ray diffraction data to 2.96 A Ê resolution collected from a native crystal at the Photon Factory (Tsukuba, Japan) showed that the crystal belonged to the hexagonal space group P6 5 22, with unit-cell parameters a = b = 136.15, c = 363.46 A Ê . The asymmetric unit of the crystal contained four DyP molecules, with a corresponding Matthews coef®cient (V M ) of 2.50 A Ê 3 Da À1 and a solvent content of 51%. Heavy-atom derivatives of DyP have been obtained and electron-density maps have been calculated. The haem is visible and continuous electron density between the haem and protein clearly indicates the location of the proximal histidine ligand.

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“…In 1999, a novel heme-containing enzyme was identified in the fungus Bjerkandera adusta (formerly Geotrichum candidum) [6,7]. This fungal enzyme bore no homology to any of the known peroxidases and was named DyP after its ability to efficiently catalyze the decolorization of a wide range of industrial dyes, particularly anthraquinone derivatives, such as Reactive Blue 5, which are poor substrates for other peroxidases [8][9][10].…”

Section: Introductionmentioning

confidence: 99%

The multihued palette of dye-decolorizing peroxidases

Singh¹,

Eltis²

2015

Archives of Biochemistry and Biophysics

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Decolorization of molasses and a dye by a newly isolated strain of the fungusGeotrichum candidum Dec 1

Cited by 64 publications

References 11 publications

Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus

Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus

A unique dye-decolorizing peroxidase, DyP, fromThanatephorus cucumerisDec 1: heterologous expression, crystallization and preliminary X-ray analysis

The multihued palette of dye-decolorizing peroxidases

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