THERMODYNAMICS AND KINETICS OF THERMO-INACTIVATION AND REGENERATION OF PARTIALLY PURIFIED PEROXIDASE FROM GONGRONEMA LATIFOLIUM LEAVES
ABSTRACT Peroxidase activity from G. latifolium was done to see whether it could be used in industries. Crude peroxidase was extracted from G. latifolium with 0.05M sodium phosphate buffer of pH 6.0; 70% ammonium sulphate  saturation to  precipitated  protein with the  highest  G.  latifolium  peroxidase activity.  After  gel  filtration,  two  major  peaks  were  seen  and  the  active  fractions were  pooled differently together and characterized. The optimal pH for the enzyme ...
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