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Preparation of enzyme‐in‐polymer composites with high activity and stability
Author(s) -
Kim Jungbae,
Kosto Timothy J.,
Manimala Joseph C.,
Nauman E. Bruce,
Dordick Jonathan S.
Publication year - 2001
Publication title -
aiche journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.958
H-Index - 167
eISSN - 1547-5905
pISSN - 0001-1541
DOI - 10.1002/aic.690470124
Subject(s) - glutaraldehyde , aqueous solution , chymotrypsin , polymer , polyethylene , composite number , immobilized enzyme , chemistry , solvent , toluene , chemical engineering , materials science , organic chemistry , composite material , enzyme , trypsin , engineering
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 α‐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.