Title of article :
Covalent immobilization of enzymes within micro-aqueous organic media
Author/Authors :
Zhu، نويسنده , , Xiongjun and Zhou، نويسنده , , Tao and Wu، نويسنده , , Xiuxiu and Cai، نويسنده , , Yixuan and Yao، نويسنده , , Dongsheng and Xie، نويسنده , , Chunfang and Liu، نويسنده , , Daling، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2011
Abstract :
Traditional covalent immobilization of enzymes was mostly operated within water phase. However, most of enzymes are flexible when they are in water environment, and the covalent reactions generally lead to complete or partial activity losing due to the protein conformational changes.
aper examined enzyme covalent immobilization operated in micro-aqueous organic media, to display the differences between two environments of immobilization within water and micro-aqueous organic solvent by activity and stability determination of the resulting immobilized enzymes. Catalase, trypsin, horseradish peroxidase, laccase and glucose oxidase have been employed as model enzymes. Results showed the thermal, pH and reusable stabilities of the micro-aqueous organic covalently immobilized enzymes were improved when compared with the immobilized enzymes within water. Micro-aqueous covalent immobilization showed a remarkable advantage in remaining the enzymes catalytic activity for all the five enzymes compared with the traditional water phase immobilization. And the optimum pH values for both immobilization within water and micro-aqueous organic media shifted slightly.
Keywords :
Covalent immobilization , Micro-aqueous immobilization , Conformation memory , Enzyme , Micro-aqueous organic solvent
Journal title :
Journal of Molecular Catalysis B Enzymatic
Journal title :
Journal of Molecular Catalysis B Enzymatic