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Improved nonporous magnetic supports for immobilized enzymes
Author(s) -
Halling P. J.,
Dunnill P.
Publication year - 1979
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.260210304
Subject(s) - glutaraldehyde , adsorption , chemical engineering , immobilized enzyme , covalent bond , silane , desorption , chemistry , substrate (aquarium) , materials science , corrosion , chromatography , organic chemistry , enzyme , geology , oceanography , engineering
Ni powders coated by deposition of TiO 2 or controlled oxidation to NiO develop substantial resistance to corrosion. Chymotrypsin immobilized to these coated Ni supports shows very high stability of activity on storage. Chymotrypsin immobilized by adsorption and glutaraldehyde crosslinking was fairly rapidly eluted under operational conditions in the presence of substrate. If 3‐aminopropyltriethoxysilane (APS) was used to produce a covalent linkage, desorption of enzyme still occurred because of relatively unstable bonding of the silane to the oxide surface. A more stable attachment was produced by joining together many silane links with a layer of polyglutaraldehyde. The mechanism of action of APS as a coupling agent under these conditions is discussed. γ‐Fe 2 O 3 , and particularly a Mn‐Zn ferrite, are suitable magnetic support materials available with smaller particle sizes. Particles below 1 μm give the expected higher specific activities of immobilized enzymes.