alpha-chymotrypsin and tetramethoxysilane

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.

Topics: Chromatography, Gas; Chymotrypsin; Enzyme Stability; Enzymes, Immobilized; Esterification; Kinetics; Protein Conformation; Serine Endopeptidases; Silanes; Solvents; Sonication; Subtilisin; Trypsin