Recently, enzymatic treatment using peroxidases in removal of aromatic compounds has gained importance. In this study pointed gourd peroxidase was salt fractionated and direct immobilization of these proteins on diethylaminoethyl cellulose for oxidation of phenol and α-naphthol has been investigated. The activated diethylaminoethyl cellulose was quite effective in high yield immobilization of peroxidases from pointed gourd and it could bind ~576 units per g of the matrix. Immobilized pointed gourd peroxidase on this anion exchanger showed very high effectiveness factor 'Ɛ' as 0.91 with an activity yield of 91%. Immobilized PGP (I-PGP) as compared to soluble counterparts (s-PGP) were more effective and removed 79%, 88% and 54% oxidation of phenol and α-naphthol by 75%, 81% and 61% at 30, 40 and 50°C respectively, with a treatment time of 140 min. In the absence CdCl2 s-PGP as well as I-PGP exhibited upto 93% of oxidation of these compounds; whereas the presence of CdCl2 of negatively affected the removal of phenol and α-naphthol. The reactor worked well continuously for over one month for effectively oxidizing/ removing phenol and α-naphthol by 54% and 61% respectively. Thus, such immobilized enzyme systems in reactor have a great future and could be exploited for treating organic pollutants present in industrial effluents.