Investigation of theα-amylase immobilization
Abstract: Enzyme, as a biological catalyst, is widely used in food processing, pharmaceuticals and fine chemical industries for its high selectivity, mild reaction, non-pollutaion and other good characteristics. With people's increasing attention to the environmental protection, the application of enzyme will be more concerned. However, there are many shortcomings of free enzyme, such as poor stability, easy deactivation, non-reuse, difficultly purification and so on. It is more difficult in wide range of industrial applications.. Under these conditions, the concepts and techniques of immobilization of enzyme are mentioned and developed. In addition, use of natural polymer carrier and its modification, or use of some advanced technology, such as supercritical technology, nanometer technology, membrane technology to immobilize enzyme have become interesting topics on enzymatic engineering.
α-amylase was immobilized on polystyrene anion-exchange resin as support by two means, one is adsorption the other is adsorption and cross-linking. The conditions of immobilization were investigated. The optimum conditions for the immobilization were as follows: α-amylase was immobilized on polystyrene anion-exchange resin for 16h in 6~9℃ and pH 6.8,then cross-linked with 4% glutaraldehyde for 8h in 6~9℃. The stability of immobilized α-amylase is better in cross-linking, to overcome the traditional adsorption of shortcomings, and increase pH stability, thermal stability and operation stability of the immobilized α-amylase.
