The N-benzoyl-L-tyrosine ethyl ester (BTEE) anchored in cyclodextrin (β and β-methyl CD) serves as an excellent substrate for subtilisin Carlsberg catalysis. The rate of hydrolysis was found to be approximately twofold higher than that of the methanolic substrate. The K(mapp) and V(max) values for the CD anchored substrates were significantly higher than the methanol- solubilized BTEE.
|Original language||English (US)|
|Number of pages||9|
|Journal||Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology|
|State||Published - 1998|
All Science Journal Classification (ASJC) codes
- Applied Microbiology and Biotechnology
- Molecular Biology