Premium
Immobilization of glucoamylase and glucose oxidase in activated carbon: Effects of particle size and immobilization conditions on enzyme activity and effectiveness
Author(s) -
Bailey James E.,
Cho Y. K.
Publication year - 1983
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260250803
Subject(s) - glucose oxidase , activated carbon , chemistry , particle size , enzyme , immobilized enzyme , biochemistry , chemical engineering , organic chemistry , adsorption , engineering
Glucoamylase and glucose oxidase have been immobilized on carbodiimide‐treated activated carbon particles of various sizes. Loading data indicate nonuniform distribution of immobilized enzyme within the porous support particles. Catalysts with different enzyme loading and overall activities have been prepared by varying enzyme concentration in the immobilizing solution. Analysis of these results by a new method based entirely upon experimentally observable catalyst properties indicates that intrinsic catalytic activity is reduced by immobilization of both enzymes. Immobilized glucoamylase intrinsic activity decreases with increasing enzyme loading, and similar behavior is suggested by immobilized glucose oxidase data analysis. The overall activity data interpretation method should prove useful in other immobilized enzyme characterization research, especially in situations where the intraparticle distribution of immobilized enzyme is nonuniform and unknown.