Purification and Characterization of a Novel Peroxidase from Geotrichum candidum Dec 1 Involved in Decolorization of Dyes

Abstract

A peroxidase (DyP) involved in the decolorization of dyes and produced by the fungus strain Geotrichum candidum Dec 1 was purified. DyP, a glycoprotein, is glycosylated withN-acetylglucosamine and mannose (17%) and has a molecular mass of 60 kDa and an isoelectric point (pI) of 3.8. The absorption spectrum of DyP exhibited a Soret band at 406 nm corresponding to a hemoprotein, and its Na2S2O4-reduced form revealed a peak at 556 nm that indicates the presence of a protoheme as its prosthetic group. Nine of the 21 types of dyes that were decolorized by Dec 1 cells were decolorized by DyP; in particular, anthraquinone dyes were highly decolorized. DyP also oxidized 2,6-dimethoxyphenol and guaiacol but not veratryl alcohol. The optimal temperature for DyP activity was 30°C, and DyP activity was stable even after incubation at 50°C for 11 h.

Crystal structures of dye‐decolorizing peroxidase with ascorbic acid and 2,6‐dimethoxyphenol

“…The first member of this family identified was DyP from Bjerkandera adusta Dec 1, which was found to decolorize dye wastewater. DyP differed from other peroxidases in that it could oxidize anthraquinone compounds [11], had a different primary structure than all other peroxidases [12], and did not have well conserved amino acids around the heme moiety [13]. Several genes homologous to DyP have been identified and classified as a novel heme peroxidase family, DyP-type peroxidase.…”

DyP-type Peroxidases: A Promising and Versatile Class of Enzymes

“…Dye-decolorizing (DyP-type) peroxidases were first discovered in fungi and are named after their ability to degrade a wide range of dyes [6]. Subsequently, additional members were found in the proteomes of other fungi, as well as in several bacteria [7].…”

“…Hemecontaining peroxidases were originally classified into two superfamilies: the plant peroxidases and animal peroxidases [4]. Remarkably, some members of the peroxidase superfamily have been studied for more than a century like, for example, Horseradish Peroxidase (HRP) [5], and in this respect, it was highly fascinating that the first member of a newly discovered peroxidase superfamily, the group of DyP-type peroxidases, was described in the late 90's [6]. Here, we will discuss the biochemical and structural features of DyP-type peroxidases, as well as their promising biotechnological potential.…”

A new peroxidase from garlic (Allium sativum) bulb: its use in H2O2 biosensing

“…In fact, POX 1B retained full activity after 40 min incubation at 40 • C as well as at 50 • C. At 60 • C, 90 % of activity was retained after 20 min, but 70 % of the initial activity was lost after 40 min incubation. POX 1B exhibits the same stability against temperature as HRP [51][52][53]. However, POX 1B is more stable than POX 2 , since this enzyme lost 50 % of its activity after 15 min incubation at 60 • C [25].…”