An Economical and Simple Bioaffinity Support for the Immobilization and Stabilization of Tomato (Lycopersicon Esculentum) Peroxidase
Mahreen Matto, Sarah Naqash and Qayyum Husain*
Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim
University, Aligarh-202002. INDIA
* Corresponding author: E-mail: email@example.com; firstname.lastname@example.org,
Phone No. (R) # 91-571-2720135; (O) # 91-571-2700741; Fax No. # 91-571-2721776
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.
Keywords: Ammonium sulphate, concanavalin A, cellulose, tomato, Lycopersicon esculentum, immobilization.