Catalytic activity of Teflon particle-immobilized protease in aqueous solution
2000
α-Chymotrypsin (Chy) was entrapped in polytetrafluoroethylene (PTFE) particles. The entrapped enzyme showed twofold catalytic activity for amino acid ester hydrolysis in aqueous solution than free enzyme. The Chy/PTFE particles also catalyzed the peptide synthesis in aqueous solution with a yield of 14%. Both the synthetic and the hydrolytic activities of the entrapped enzyme were enhanced as compared with the free enzyme. The PTFE matrix should provide the enzyme molecules by creating a hydrophobic environment which results in enhanced peptide synthesis in aqueous solution.
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