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

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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.
Original languageUndefined
Pages (from-to)553-556
JournalBiotechnology and bioengineering
Volume59
Issue number59
DOIs
Publication statusPublished - 1998

Keywords

  • METIS-105986
  • IR-11085
  • α-chymotrypsin
  • proteases
  • organic solvents
  • enzymatic peptide synthesis
  • 18-crown-6

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