Document Details Document Type : Article In Journal  Document Title : Characterisation of an anionic peroxidase from horseradish cv. Balady Characterisation of an anionic peroxidase from horseradish cv. Balady   Subject : Biochemistry  Document Language : English  Abstract : 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 exhibited more than 50% of activity in the pH range between 4.0 and 8.0 with its pH optimum at 5.5. Several metal cations had partial inhibitory effects toward POIII. Fe3+ enhanced the activity of the enzyme by 160% at 5 mM. All the metal chelators caused partial inhibitory effects toward POIII, except for EDTA at 1 mM, which had no effect on the enzyme.  ISSN : 0308-8146  Journal Name : Food Chemistry  Volume : 128  Issue Number : 3  Publishing Year : 1432 AH 2011 AD  Article Type : Article  Added Date : Monday, February 13, 2012  Researchers Researcher Name (Arabic) Researcher Name (English) Researcher Type Dr Grade Email صالح أحمد محمد Mohamed, Saleh Ahmed Researcher Doctorate saleh38@hotmail.com خالد عمر أبو النجا Abulnaja, Khalid O Researcher Doctorate kabualnaja@kau.edu.sa عاطف سعدي عدس Ads, Atef S Researcher Doctorate   جلال الدين أعظم جلال خان Khan, Jalaluddin A J Researcher Doctorate jjalal@kau.edu.sa طه عبدالله قمصاني Kumosani, Taha Abdullah Researcher Doctorate tkumosani@kau.edu.sa Files File Name Type Description  32276.pdf pdf Abstract Back To Researches Page