Large acceleration of α-chymotrypsin-catalyzed dipeptide formation by 18-crown-6 in organic solvents

Unen van, Dirk-Jan and Engbersen, Johan F.J. and Reinhoudt, David N. (1998) Large acceleration of α-chymotrypsin-catalyzed dipeptide formation by 18-crown-6 in organic solvents. Biotechnology and Bioengineering, 59 (5). pp. 553-556. ISSN 0006-3592

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Abstract:	The effects of 18-crown-6 on the synthesis of peptides catalyzed by α-chymotrypsin are reported. Lyophilization of the enzyme in the presence of 50 equivalents of 18-crown-6 results in a 425-fold enhanced activity when the reaction between the 2-chloroethylester of N-acetyl-L-phenylalanine and L-phenylalaninamide is carried out in acetonitrile. Addition of crown ether renders the dipeptide synthesis in nonaqueous solvents catalyzed by α-chymotrypsin possible on a preparative scale. The acceleration is observed in different solvents and for various peptide precursors.
Item Type:	Article
Copyright:	© 1998 Wiley
Faculty:	Science and Technology (TNW)
Research Group:	Biomedical Chemistry (BMC)
Link to this item:	http://purl.utwente.nl/publications/11085
Official URL:	http://dx.doi.org/10.1002/(SICI)1097-0290(19980905)59:5<553::AID-BIT4>3.0.CO;2-9
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