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Immobilization of proteins by reductive alkylation with hydrophobic aldehydes (1981)

Wu, Hua-Lin ; Means, Gary E.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 23 (1981), S. 855-861

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ISSN: 0006-3592

Keywords: Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: 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.

Additional Material: 1 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/bit.260230415

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