Purification of a peroxidase from Solanum melongena fruit juice.
Solanum melongena fruit juice contains peroxidase activity of the order of 0.125 IU/mL. A method for the 11-fold purification of the enzyme was developed. The Km values of the peroxidase for the substrates guaiacol and hydrogen peroxide were 6.5 mM and 0.33 mM, respectively. The pH and temperature optima were 5.5 and 84 degrees C, respectively using guaiacol as the substrate. Sodium azide and phenyl hydrazine inhibited the enzyme competitively.
Vernwal
S K
SK
Department of Chemistry, D D U Gorakhpur University, Gorakhpur 273 009, India.
Yadav
R S S
RS
Yadav
K D S
KD
D001628:Beverages; D004305:Dose-Response Relationship, Drug; D005638:Fruit; D006139:Guaiacol / Q000494:pharmacology; D006861:Hydrogen Peroxide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010544:Peroxidases / Q000737:chemistry*; D010659:Phenylhydrazines / Q000494:pharmacology; D019810:Sodium Azide / Q000494:pharmacology; D032323:Solanum melongena / Q000201:enzymology*; D013696:Temperature
D010659:Phenylhydrazines; C030299:phenylhydrazine; D006139:Guaiacol; D019810:Sodium Azide; D006861:Hydrogen Peroxide; D010544:Peroxidases