Activity and Stability of Urease Enzyme Immobilized on Amberlite Resin

Abstract

Immobilization of enzymes is a good field of study to expand the life of enzyme in and lowering the cost of the chemical processes such as separation processes. Urease is an important enzyme with medical and industrial applications. The aim of the present study is to prepare an immobilized urease on a strong cation exchange resin (Amberlite IR120 -Na) and study of its activity and stability. We monitored the liberation of Na ions in the collected fractions and searching for protein in the fractions as an indicators of immobilization by ion exchange phenomenon. Sodium is measured using atomic absorption spectroscopy techniques, while protein tested by Bradford’s method. Immobilized urease activity was evaluated by salicylate-hypochlorite method. The results indicated a complete immobilization of urease enzyme on the resin surface with reserving 92% of the activity of free enzyme. The immobilized urease enzyme on resin showed good stability and it has a 62% of its activity after 154 days of storage at room temperature. It is concluded that a new immobilized urease enzyme system is prepared with good enzyme activity and stability.

Surface Gelatin-Coated β-Mannanase-Immobilized Lignin for Delayed Release of β-Mannanase to Remediate Guar-Based Fracturing Fluid Damage

“…The quantity of β-mannanase immobilized on the surface of lignin was determined based on the Bradford method by measuring the initial and final quantities of β-mannanase in the immobilization medium. 20 Bsa solution at known concentrations was calibrated to calculate binding levels. The encapsulation efficiency (EE) of gelatin for MIL was determined using the following eq 2 where EE is the percentage encapsulation of the Ge@MIL, Q MIL is the quantity of MIL encapsulated in Ge@MIL (g), and Q total is the quantity of MIL added for encapsulation (g).…”