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High‐yield method for immobilization of enzymes
Author(s) -
Wasserman Bruce P.,
Hultin Herbert O.,
Jacobson Bruce S.
Publication year - 1980
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.260220203
Subject(s) - glucose oxidase , glutaraldehyde , immobilized enzyme , aspergillus niger , chemistry , enzyme , chromatography , adsorption , yield (engineering) , polyethylenimine , catalase , nuclear chemistry , biochemistry , organic chemistry , materials science , transfection , metallurgy , gene
Two types of polyethylenimine‐coated glass microbeads (13–44 μm) were synthesized and used for the immobilization of glucose oxidase from Aspergillus niger and catalase from A. niger and beef liver. The two types of beads were distinguishable by differences in their surface topography. Immobilizations were performed by adsorption followed by treatment with glutaraldehyde. The immobilized‐enzyme activities per unit support of all of the enzymes tested were compared with and found to be superior to the immobilized activities attainable on aminopropyl‐activated glass microbeads. When enzyme was present in less than saturating amounts, the coated beads were able to remove 100% of the glucose oxidase activity initially present in the immobilization solution, with 78–87% of that activity expressed on the support surface. Bound glucose oxidase was more stable to thermal inactivation than native enzyme.