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Sol-gel immobilization of serine proteases for application in organic solvents
D J van Unen1, J F Engbersen, D N Reinhoudt
1Laboratory of Supramolecular Chemistry and Technology, MESA Research Institute, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands.
Abstract:
The serine proteases alpha-chymotrypsin, trypsin, and subtilisin Carlsberg were immobilized in a sol-gel matrix and the effects on the enzyme activity in organic media are evaluated. The percentage of immobilized enzyme is 90% in the case of alpha-chymotrypsin and the resulting specific enzyme activity in the transesterification of N-acetyl-L-phenylalanine ethyl ester with 1-propanol in cyclohexane is 43 times higher than that of a nonimmobilized lyophilized alpha-chymotrypsin. The activities of trypsin and subtilisin Carlsberg are enhanced with 437 and 31 times, respectively. The effect of immobilization on the enzyme activity is highest in hydrophobic solvents.