Adsorption of polyphenol oxidases on Celite 545 directly from ammonium sulphate fractionated proteins of brinjal (<i style="">Solanum melongena</i>)

Abstract

Partially purified polyphenol oxidase (PPO) from brinjal <i style="">(Solanum melongena)</i> was immobilized on the Celite 545 by simple adsorption at pH 7.0. Celite adsorbed 248 EU of PPO per g of the matrix.<b style=""> </b>Immobilized enzyme preparation exhibited: effectiveness factor ‘<img src='/image/spc_char/Etta.gif'>’, 0.62; optimum pH, 9.0; and temp, 40-50^oC. Celite bound PPO retained high stability against thermal denaturation as compared to soluble counterpart. Urea and water-miscible organic solvent treatment significantly enhanced the activity of brinjal PPO; enhancement was significantly more pronounced in case of immobilized enzyme preparation. Celite bound brinjal PPO had no loss in enzyme activity even when exposed to very high amount of trypsin. Immobilized PPO preparation exhibited a marked resistance against inactivation mediated by washing detergents such as Surf Excel and Rin Powder.