Temperature effects on enzyme activity of chicken liver esterase used in calorimetric biosensor.

Abstract

The temperature effects on enzyme activity at the conditions with and without inhibition, operation, and storage were investigated for free esterase and immobilized chicken liver esterase with three methods (adsorption, adsorption-microcapsule, and adsorption-crosslinking) used in a calorimetric biosensor. The results indicated that the temperature had significant effects on the enzyme activity by means of catalytic reaction, irreversible denaturation, mass transfer, and structure deformation of resin. Among all the esterase, the adsorption-crosslinking immobilized esterase had the best performances of enzyme activity retention ratio (EARR), above 96% in operation and 90% in storage on condition of maintaining its response to dichlorvos.