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Immobilization of enzymes on magnetic particles
Author(s) -
Van Leemputten E.,
Horisberger M.
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.260160308
Subject(s) - invertase , glutaraldehyde , trypsin , chemistry , raffinose , immobilized enzyme , chromatography , enzyme , esterase , sucrose , yield (engineering) , biochemistry , materials science , metallurgy
Trypsin (EC 3.4.4.4) was immobilized in low yield on aminoalkylsilylated magnetite (Fe 3 O 4 ). Better results were obtained when trypsin was immobilized by crosslinking with glutaraldehyde on magnetite. The preparation contained 36 mg protein/g magnetite and the enzyme retained 46% and 11% of esterase and proteolytic activity. Immobilized trypsin was more heat stable than trypsin. Invertase (β‐ D ‐fructofuranoside fructohydrolase, EC 3.2.1.26) was cross‐linked on magnetite with glutaraldehyde in low yield due to the inactivation of the enzyme. However in the presence of 1% sucrose, the total activity recovered was 79% of the initial activity and the preparation contained 4.4 mg/g of active invertase. Immobilized invertase was less active than invertase when acting on oligosaccharides of the raffinose family. The immobilized enzymes could be easily recovered, from solutions or suspensions, magnetically.