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Immobilized enzyme reaction stability: Attrition of the support material
Author(s) -
Regan D. L.,
Dunnill P.,
Lilly M. D.
Publication year - 1974
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.260160304
Subject(s) - immobilized enzyme , chemistry , chemical engineering , bioreactor , continuous reactor , particle size , particle (ecology) , covalent bond , enzyme , chromatography , organic chemistry , catalysis , biology , ecology , engineering
One of the main reasons for immobilizing an enzyme is to enable its reuse, or continuous use, in a reactor. Consequently immobilized enzyme stability is an important factor in enzyme reactor design. The performance of the reactor will decrease if during operation the support material disintegrates into smaller particles that pass out of the reactor system. When β‐galactosidase is immobilized by covalent attachment to AE‐cellulose, the smaller particles have a higher activity. After subjection of the immobilized enxyme to a shear stress the average particle size decreases and the total enzymic activity increases. A loss of small particles from the reactor, although constituting a small weight percent loss of support, will result in a disproportionately large loss in activity. The relevance of these observations to reactor performance is discussed.