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Saccharomonospora viridis  is a thermophilic actinomycete that may have biotechnological applications because of its dye decolorizing activity, though the enzymatic oxidative system responsible for this activity remains elusive. Bioinformatic analysis revealed a DyP-type peroxidase gene in the genome of  S. viridis  DSM 43017 with sequence similarity to peroxidase from dye-decolorizing microbes. This gene,  svidyp , consists of 1,215 bp encoding a polypeptide of 404 amino acids. The gene encoding  Svi DyP was cloned, heterologously expressed in  Escherichia coli , and then purified. The recombinant protein could efficiently decolorize several triarylmethane dyes, anthraquinonic and azo dyes under neutral to alkaline conditions. The optimum pH and temperature for  Svi DyP was pH 7.0 and 70°C, respectively. Compared with other DyP-type peroxidases,  Svi DyP was more active at high temperatures, retaining>63% of its maximum activity at 50–80°C. It also showed broad pH adaptability (>35% activity at pH 4.0–9.0) and alkali-tolerance (>80% activity after incubation at pH 5–10 for 1 h at 37°C), and was highly thermostable (>60% activity after incubation at 70°C for 2 h at pH 7.0).  Svi DyP had an accelerated action during the biobleaching of eucalyptus kraft pulp, resulting in a 21.8% reduction in kappa number and an increase of 2.98% (ISO) in brightness. These favorable properties make  Svi DyP peroxidase a promising enzyme for use in the pulp and paper industries.

plos one

Application of a Novel Alkali-Tolerant Thermostable DyP-Type Peroxidase from Saccharomonospora viridis DSM 43017 in Biobleaching of Eucalyptus Kraft Pulp