Abstract
The serine proteases α-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 α-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 α-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.
Original language | Undefined |
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Pages (from-to) | 154-158 |
Journal | Biotechnology and bioengineering |
Volume | 75 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2001 |
Keywords
- organic solvents
- serine proteases
- Sol-gel
- IR-59871
- immobilization
- METIS-202976
- Transesterification