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Immobilization of proteins by reductive alkylation with hydrophobic aldehydes
Author(s) -
Wu HuaLin,
Means Gary E.
Publication year - 1981
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.260230415
Subject(s) - sodium cyanoborohydride , chemistry , alkylation , hydrolysis , yeast , yield (engineering) , trypsin , alcohol dehydrogenase , enzyme , immobilized enzyme , sepharose , chromatography , organic chemistry , hydrophobic effect , biochemistry , combinatorial chemistry , catalysis , materials science , metallurgy
A new method is described for the immobilization of enzymes and other proteins onto hydrophobic gels. Trypsin, for example, can be quantitatively immobilized by reaction with sodium cyanoborohydride and dodecyladehyde‐coated Octyl‐Sepharose. Noncovalent interactions between the hydrophobic gel and approximately 10 resulting dodecylamino groups in the modified enzyme bind it very strongly but do not affect its ability to hydrolyze benzolarginine ethyl ester. The same procedure can also be used to immobilize E. Coli asparaginase and yeast alcohol dehydrogenase in high yield.