Enzyme stabilization by bilayer "encagement"

R. Tor, Y. Dror, A. Freeman

Research output: Contribution to journalArticlepeer-review

Abstract

A two-step simple procedure for enzyme stabilization-in solution-was developed. The enzyme is first coated, in a complementary way, by a monolayer of low-molecular-weight polymeric glutaraldehyde. Following removal of unbound polyaldehyde, this layer is crosslinked by a second layer made of polyacrylamide derivatives, bearing primary amine or acylhydrazide groups. Thus a bilayered, chemically crosslinked, synthetic "cage" is formed, surrounding the enzyme and increasing its stability to denaturation by rigidification of its structure. The "encagement" process results in a significant enhancement of the thermal stability as well as survival in the presence of water-miscible organic solvents. The "encaged," stabilized enzyme could be readily immobilized by crosslinking into polyacrylamide-hydrazide gel, resulting in an additional stabilization effect imposed by this gel. The procedure worked out was demonstrated by the stabilization of two enzymes of analytical importance [glucose oxidase (E.C.1.1.3.4) and penicillinase (E.C.3.5.2.6)] as well as dramatic stabilization of carboxylesterase (from pig liver, E.C.3.1.1.1) one of the most useful enzymes in bio-organic synthesis.

Original languageEnglish
Pages (from-to)306-312
Number of pages7
JournalEnzyme and Microbial Technology
Volume11
Issue number5
DOIs
StatePublished - May 1989

Keywords

  • Enzyme stabilization
  • enzyme immobilization

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