An Economical and Simple Bioaffinity Support for the Immobilization and Stabilization of Tomato (Lycopersicon Esculentum) Peroxidase

Ammonium sulphate fractionated tomato proteins were used for the direct immobilization of peroxidase on bioaffinity, Con A-cellulose support. Con A-cellulose bound peroxidase retained 77% of the original activity. The immobilized enzyme showed very high stability against denaturation mediated by heat, pH, organic solvents and inhibitors. Soluble and immobilized peroxidase exhibited maximum activity at 40 °C and pH 6.0. Con A-cellulose bound peroxidase retained 44% and 51% activity against the exposure to 50% DMF and n-propanol for 1 h, respectively; however soluble enzyme showed only 21% and 20% activity under similar exposure to organic solvents, DMF and n-propanol. Immobilized peroxidase retained significantly higher activity against sodium azide and sodium sulphite as compared to soluble enzyme.