Cloning, characterization and paper pulp applications of a newly isolated DyP type peroxidase from Rhodococcus sp. T1

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ŞAHİNKAYA M., Colak D. N. , Ozer A. , ÇANAKÇI S. , DENİZ İ. , BELDÜZ A. O.

MOLECULAR BIOLOGY REPORTS, vol.46, no.1, pp.569-580, 2019 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 46 Issue: 1
  • Publication Date: 2019
  • Doi Number: 10.1007/s11033-018-4509-9
  • Page Numbers: pp.569-580


A newly identified ligninolytic Rhodococcus strain (Rhodococcus sp. T1) was isolated from forestry wastes (Trabzon/Turkey). The DyP type peroxidase of Rhodococcus sp. T1 (DyPT1) was cloned, characterized and paper treated for industrial applications. Molecular weight of the protein was about 38kDa. The kinetic parameters were 0.94mM and 1417.53 mu mol/min/mg for Km and Vmax, respectively. The enzyme was active at the temperature range of 25-65 degrees C and optimum temperature was 35 degrees C, enzyme was stable up to 6 days at room temperature. Optimum pH of the DyPT1 was 4.0 and it was stable between pH 4.0-6.0 up to 8 days at room temperature. Effects of some metal ions, Hemin, and some chemical agents on DyPT1 were determined. Hemin has implemented protective effects on the stability and the activity of the enzyme in long time periods when added into growing medium. DyPT1 was applied to eucalyptus kraft pulp for analyzing the bleaching efficiency, physical and optical tests of the manufuctared paper were carried out. Application of lignin peroxidase to kraft pulp caused a decrease of 5.2 units for kappa number and an increase from 52.05 to 64.18% in the delignification rate.