Preparation of enzyme-in-polymer composites with high activity and stability

Jungbae Kim, Timothy J. Kosto, Joseph C. Manimala, E. Bruce Nauman, Jonathan S. Dordick

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


Flash devolatilization was applied to incorporate an enzyme into a polymer matrix; which created a novel and highly active biocatalytic composite suitable for use in both aqueous and organic media. Enzymes were codissolved in toluene with commercial, high-molecular-weight polymers, and the solvent was then rapidly removed by injecting the mixture into a vacuum chamber. Subsequent cross-linking of the enzyme with glutaraldehyde resulted in stable entrapped enzyme within the polymeric matrices. For example, a composite of β-chymotrypsin and low-density polyethylene showed no significant loss of enzymatic activity in aqueous buffer over a period of one month. The normalized activity of this biocatalytic material in organic solvents was 3-13 times higher than that of native α-chymotrypsin lyophilized from aqueous buffer. Washing the composite material with aqueous buffer increased the activity in isooctane an additional ten fold. The composites of α-chymotrypsin and polyethylene demonstrated the feasibility of obtaining active and stable biocatalytic materials via the application of compositional quenching to a biological system.

Original languageEnglish
Pages (from-to)240-244
Number of pages5
JournalAIChE Journal
Issue number1
Publication statusPublished - 2001 Jan
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Environmental Engineering
  • General Chemical Engineering


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