Enzyme-Carrying Polymeric Nanofibers Prepared via Electrospinning for Use as Unique Biocatalysts
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- 作者：Hongfei Jia ; Guangyu Zhu ; Bradley Vugrinovich ; Woraphon Kataphinan ; Darrell H. Reneker ; and Ping Wang
- 刊名：Biotechnology Progress
- 出版年：2002
- 出版时间：October 2002
- 年：2002
- 卷：18
- 期：5
- 页码：1027 - 1032
- 全文大小：112K
- 年卷期：v.18,no.5(October 2002)
- ISSN：1520-6033
文摘
Improvement of catalytic efficiency of immobilized enzymes via materials engineeringwas demonstrated through the preparation of bioactive nanofibers. Bioactive polystyrene (PS) nanofibers with a typical diameter of 120 nm were prepared and examinedfor catalytic efficiency for biotransformations. The nanofibers were produced byelectrospinning functionalized PS, followed by the chemical attachment of a modelenzyme, 
-chymotrypsin. The observed enzyme loading as determined by active sitetitration was up to 1.4% (wt/wt), corresponding to over 27.4% monolayer coverage ofthe external surface of nanofibers. The apparent hydrolytic activity of the nanofibrousenzyme in aqueous solutions was over 65% of that of the native enzyme, indicating ahigh catalytic efficiency as compared to other forms of immobilized enzymes.Furthermore, nanofibrous -chymotrypsin exhibited a much-improved nonaqueousactivity that was over 3 orders of magnitude higher than that of its native counterpartsuspended in organic solvents including hexane and isooctane. It appeared that thecovalent 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 thanthat of the native enzyme.
-chymotrypsin. The observed enzyme loading as determined by active sitetitration was up to 1.4% (wt/wt), corresponding to over 27.4% monolayer coverage ofthe external surface of nanofibers. The apparent hydrolytic activity of the nanofibrousenzyme in aqueous solutions was over 65% of that of the native enzyme, indicating ahigh catalytic efficiency as compared to other forms of immobilized enzymes.Furthermore, nanofibrous -chymotrypsin exhibited a much-improved nonaqueousactivity that was over 3 orders of magnitude higher than that of its native counterpartsuspended in organic solvents including hexane and isooctane. It appeared that thecovalent 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 thanthat of the native enzyme.