Muhammad Usman Amin
Preparation Of Turnip Peroxidases And Its Application To Remove The Phenolic Content Of Sannerty Effluent - 2011
Peroxidases are heme-containing oxidizing enzymes, which are wide spread in nature. They have the ability to catalyze the oxidation of many organic and inorganic electron donor substrates through a reaction with hydrogen peroxide or organic hydrogen peroxides. In this study peroxidase were purified from turnip using ammonium sulphate precipitation, poly ethylene glycol precipitation and zinc sulphate precipitations in order to find some simple and less expensive procedure for partial purification of peroxidases. Ammonium sulphate and PEG (6000) in the presence and absence of NaCl were used to make aqueous two phase system. Aqueous two-phase system (ATPS) without NaCl purified enzyme most efficiently. (NH4)2SO4 layer was subjected to dialysis and for further purification on sephadex gel which gave maximum enzyme activity of 1544u/mg protein. SD-PAGE analysis was done to determine enzyme purity. Purified enzyme was charged into the tannery waste water along with H2O2 to remove toxic phenolic content up to 98.24%.
Institute of Biochemistry & Biotechnology
1356,T
Preparation Of Turnip Peroxidases And Its Application To Remove The Phenolic Content Of Sannerty Effluent - 2011
Peroxidases are heme-containing oxidizing enzymes, which are wide spread in nature. They have the ability to catalyze the oxidation of many organic and inorganic electron donor substrates through a reaction with hydrogen peroxide or organic hydrogen peroxides. In this study peroxidase were purified from turnip using ammonium sulphate precipitation, poly ethylene glycol precipitation and zinc sulphate precipitations in order to find some simple and less expensive procedure for partial purification of peroxidases. Ammonium sulphate and PEG (6000) in the presence and absence of NaCl were used to make aqueous two phase system. Aqueous two-phase system (ATPS) without NaCl purified enzyme most efficiently. (NH4)2SO4 layer was subjected to dialysis and for further purification on sephadex gel which gave maximum enzyme activity of 1544u/mg protein. SD-PAGE analysis was done to determine enzyme purity. Purified enzyme was charged into the tannery waste water along with H2O2 to remove toxic phenolic content up to 98.24%.
Institute of Biochemistry & Biotechnology
1356,T