August 22, 2004
Conference Paper

Enzyme-polymer composites with high biocatalytic activity and stability

Abstract

We have applied vacuum-spraying and electrospinning to incorporate an enzyme into a polymer matrix, creating a novel and highly active biocatalytic composite. As a unique technical approach, enzymes were co-dissolved in toluene with polymers, and the solvent was then rapidly removed by injecting the mixture into a vacuum chamber or by electrospinning. Subsequent crosslinking of the enzyme with glutaraldehyde resulted in stable entrapped enzyme within the polymeric matrices. For example, an amorphous composite of alpha-chymotrypsin and polyethylene showed no significant loss of enzymatic activity in aqueous buffer for one month. Nanofibers of alpha-chymotrypsin and polystyrene also showed no decrease in activity for more than two weeks. The normalized activity of amorphous composite in organic solvents was 3-13 times higher than that of native alpha-chymotrypsin. The activity of nanofibers was 5-7 times higher than that of amorphous composite in aqueous buffer solution. The composites of alpha-chymotrypsin and polymers demonstrate the feasibility of obtaining a wide variety of active and stable biocatalytic materials with many combinations of enzymes and polymers.

Revised: September 14, 2005 | Published: August 22, 2004

Citation

Kim J., T.J. Kosto, J.C. Manimala, E.B. Nauman, and J.S. Dordick. 2004. Enzyme-polymer composites with high biocatalytic activity and stability. In American Chemical Society Meeting 228, 228, Poly 478. Washington, District Of Columbia:American Chemical Society. PNNL-SA-43570.