Immobilization of proteins by reductive alkylation with hydrophobic aldehydes

Hua‐Lin ‐L Wu, Gary E. Means

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)855-861
Number of pages7
JournalBiotechnology and Bioengineering
Issue number4
Publication statusPublished - 1981 Apr

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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