Characterisation of an anionic peroxidase from horseradish cv. Balady

@inproceedings{Mohamed2011CharacterisationOA,
  title={Characterisation of an anionic peroxidase from horseradish cv. Balady},
  author={Saleh Abd El-aleem Mohamed and Khalid Omar Abulnaja and Atef S Ads and Jalaluddin Azam Khan and Taha Abduallah Kumosani},
  year={2011}
}
An anionic peroxidase POIII, molecular weight 56 kDa, was purified from the roots of horseradish cv. Balady. The enzyme exhibited high activity towards o-phenylenediamine and guaiacol, while o-dianisidine had moderate peroxidase activity. Pyrogallol and p-aminoantipyrine had low affinity toward POIII. POIII was found to have a temperature optimum at 40 °C; the enzyme activity remained stable up to 40 °C and retained 87%, 51% and 29% of its activity at 50, 60 and 70 °C, respectively. The enzyme… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 10 CITATIONS

Characterization of Plant Peroxidases and Their Potential for Degradation of Dyes: a Review

  • Applied Biochemistry and Biotechnology
  • 2015
VIEW 4 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED