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Enzyme‐Carrying Polymeric Nanofibers Prepared via Electrospinning for Use as Unique Biocatalysts
Author(s) -
Jia Hongfei,
Zhu Guangyu,
Vugrinovich Bradley,
Kataphinan Woraphon,
Reneker Darrell H.,
Wang Ping
Publication year - 2002
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp020042m
Subject(s) - nanofiber , electrospinning , immobilized enzyme , chemistry , catalysis , chymotrypsin , covalent bond , hydrolysis , aqueous solution , cellulase , chemical engineering , enzyme , polymer chemistry , materials science , organic chemistry , polymer , nanotechnology , trypsin , engineering
Improvement of catalytic efficiency of immobilized enzymes via materials engineering was demonstrated through the preparation of bioactive nanofibers. Bioactive polystyrene (PS) nanofibers with a typical diameter of 120 nm were prepared and examined for catalytic efficiency for biotransformations. The nanofibers were produced by electrospinning functionalized PS, followed by the chemical attachment of a model enzyme, α‐chymotrypsin. The observed enzyme loading as determined by active site titration was up to 1.4% (wt/wt), corresponding to over 27.4% monolayer coverage of the external surface of nanofibers. The apparent hydrolytic activity of the nanofibrous enzyme in aqueous solutions was over 65% of that of the native enzyme, indicating a high catalytic efficiency as compared to other forms of immobilized enzymes. Furthermore, nanofibrous α‐chymotrypsin exhibited a much‐improved nonaqueous activity that was over 3 orders of magnitude higher than that of its native counterpart suspended in organic solvents including hexane and isooctane. It appeared that the covalent binding also improved the enzyme's stability against structural denaturation, such that the half‐life of the nanofibrous enzyme in methanol was 18‐fold longer than that of the native enzyme.