Immobilization of glucoamylase on magnetic poly(styrene) particles

Citation
T. Bahar et Ss. Celebi, Immobilization of glucoamylase on magnetic poly(styrene) particles, J APPL POLY, 72(1), 1999, pp. 69-73
Citations number
17
Categorie Soggetti
Organic Chemistry/Polymer Science","Material Science & Engineering
Journal title
JOURNAL OF APPLIED POLYMER SCIENCE
ISSN journal
00218995 → ACNP
Volume
72
Issue
1
Year of publication
1999
Pages
69 - 73
Database
ISI
SICI code
0021-8995(19990404)72:1<69:IOGOMP>2.0.ZU;2-U
Abstract
Magnetic poly(styrene) particles including active groups were prepared for enzyme immobilization without any activation process. Glucoamylase, which i s widely used in industry, was immobilized onto these particles. The effect s of pH, buffer concentration, and temperature on immobilization were inves tigated; moreover, the effect of immobilization temperature on immobilized glucoamylase activity was determined for the hydrolysis of maltose. The ace tate buffer with the concentration of 6 x 10(-4) M at pH 4 and 20-30 degree s C was found as the most suitable medium for the immobilization of the glu coamylase. The amount of bound protein is 8 mg/g particle with the immobili zation yield of 70%. The maximum activity obtained with immobilized glucoam ylase is approximately 70% of the free one. (C) 1999 John Wiley & Sons, Inc .