Indian Journal Of Natural Sciences International Bimonthly ISSN: 0976 – 0997 Vol.3 / Issue 13/ August 2012 www.tnsroindia.org.in © IJONS RESEARCH ARTICLE Determination of Kinetic and Thermodynamic Parameters of Partially Purified Borassus flabellifer L.Peroxidase. Ajithadevi.K , J.Jeyasree*, R.Kalaivani , T.Williamraja, R.Indiragandhi. P. G. & Research Department of Biotechnology, Thanthai Hans Roever College, Perambalur, TamilNadu, India. Received: 15 June 2012 Revised: 14 July 2012 Accepted: 29 July 2012 *Address for correspondence J.Jeyasree Assistant Professor, Department of Biotechnology, Thanthai Hans Roever College, Perambalur - 621212 E-Mail:
[email protected] Mobile: +91- 9894241849 ABSTRACT Peroxidases are widely believed to catalyze the last enzymatic step in the biosynthesis of lignin, the dehydrogenation of the p-coumaryl alcohols. The present study was under taken to develop a system for production of peroxidase enzyme in large scale production from Borassus flabelliferL.(Arecaceae). Borassus flabellifer peroxidase was partially purified. It had single isoform. The quantity of enzyme activity and assay were determined by substrates guaiacol, O-Dianisidine, Diphenyl amine, Benzidine and Tetra methyl Benzidine. It had greater affinity towards Guaiacol compare to Benzidine and o-Dianisidine as organic substrates. The partially purified enzyme has optimum pH around 4 to 5 in presence of substrates guaiacol, o-Dianisidine, Diphenyl amine, Benzidine and Tetra methyl Benzidine. The temperature optimum for the above substrates lies in the region around 60°C. The kinetic parameters, Vmax and Km were calculated from the Michaelis-Menten plot and LB plot. A haemoprotein as it was brownish in colour. Its relative molecular weight was 100KDa and had single isoenzyme.