Hydrolysis of N — Benzoyl — L — Tyrosine Ethyl Ester Anchored in CD by α-Chymotrypsin and Subtilisin
N-Benzoyl-L-tyrosine ethyl ester (BTEE), a water insoluble substrate, was rendered soluble upon complexation with β-cyclodextrin (or its methyl derivative) and but not with γ-CD. Kinetics of the hydrolysis of such CD anchored BTEE by subtilisin Carlsberg showed a 2 to 4 fold increase in both kcat and Km values, over the methanol solubilised substrate. Whereas, α-chymotrypsin hydrolyzed the CD anchored BTEE with only a marginally higher reaction rate than the methanol solubilised BTEE.
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