Chem. J. Chinese Universities ›› 1994, Vol. 15 ›› Issue (5): 681.

• Articles • Previous Articles     Next Articles

The Activity and Thermostability of Immobilized Glucoamylase by Diazotization

KONG Wei, ZHOU Hui, WANG Li-Ping, CHEN Zun, Li Wei, SHEN Jia-Cong   

  1. Department of Molecular Biology, Jilin University, Changchun, 130023
  • Received:1993-07-27 Revised:1993-12-01 Online:1994-05-24 Published:1994-05-24

Abstract: A method getting high activity and thermostability for the immobilized glucoamylase was found out.The glucoamylase was immobilized on porous anilino-sulfonic polystyrene beads by diazotization.The effects of immobilizing pH,immobilizing time and molecular weight of the substrate on the activity and thermostability of immobilized glucoamylase were investigated.The results obtained show that by prolonging the coupling time of diazol-protein,the activity of immobilized glucoamylase got to 20000 mg/hour g dry gel,and the thermostability was 5 times higlier than that of soluble glucoamylase.

Key words: Porous ionic carrier, Immobilized enzyme, Glucoamylase

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