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Immobilization of glucoamylase on magnetic poly(styrene) particles
Author(s) -
Bahar Tahsin,
Çelebi Serdar S.
Publication year - 1999
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/(sici)1097-4628(19990404)72:1<69::aid-app7>3.0.co;2-l
Subject(s) - styrene , hydrolysis , yield (engineering) , immobilized enzyme , maltose , chemistry , magnetic nanoparticles , copolymer , nuclear chemistry , particle size , polymer chemistry , chromatography , polymer , enzyme , materials science , organic chemistry , nanoparticle , nanotechnology , metallurgy
Magnetic poly(styrene) particles including active groups were prepared for enzyme immobilization without any activation process. Glucoamylase, which is widely used in industry, was immobilized onto these particles. The effects of pH, buffer concentration, and temperature on immobilization were investigated; moreover, the effect of immobilization temperature on immobilized glucoamylase activity was determined for the hydrolysis of maltose. The acetate buffer with the concentration of 6 × 10 −4 M at pH 4 and 20–30°C was found as the most suitable medium for the immobilization of the glucoamylase. The amount of bound protein is 8 mg/g particle with the immobilization yield of 70%. The maximum activity obtained with immobilized glucoamylase is approximately 70% of the free one. © 1999 John Wiley & Sons, Inc. J Appl Polym Sci 72: 69–73, 1999