Research on the orientedly immobilized urease via concanavalin A.
- Author:
Jianqin ZHOU
1
;
Shaohua CHEN
;
Jianwen WANG
Author Information
1. School of Pharmacy, Soochow University, Suzhou 215123, China. zkzhu@ustc.edu
- Publication Type:Journal Article
- MeSH:
Chitosan;
chemistry;
Concanavalin A;
chemistry;
Enzymes, Immobilized;
Glutaral;
chemistry;
Glycoproteins;
chemistry;
Hydrogen-Ion Concentration;
Microspheres;
Temperature;
Urease;
metabolism
- From:
Chinese Journal of Biotechnology
2008;24(4):617-621
- CountryChina
- Language:Chinese
-
Abstract:
Concanavalin A (ConA) is immobilized on a pre-activated chitosan microspheres, and then oriented immobilization of urease is carried out based on the strong interaction between ConA and glycoprotein. The optimum immobilization conditions are as follows: glutaraldehyde concentration is 3.5%, ConA concentration 1 mg/mL, ConA pH 7.0 and urease concentration 0.4 mg/mL. For orientedly immobilized urease, the highest activity was allowed at pH 5.0-6.0 and temperature 77 degrees C, and the Michaelis constant (Km) was disclosed to be 11.76 mmol/L by Lineweaver-Burk plot. Compared with the free urease and the randomly immobilized urease, the optimum pH of the orientedly immobilized urease becomes smaller and the pH domain wider. Orientedly immobilized urease presents higher temperature resistance, higher affinity to the substrate, and higher stability of operation.
