Papain-catalysed synthesis of dipeptides: a novel approach using free amino acids as nucleophiles

Enzyme Microb Technol. 1990 Jan;12(1):56-60. doi: 10.1016/0141-0229(90)90181-o.

Abstract

For the first time, papain-catalysed synthesis of peptide bonds was successfully carried out using free amino acids as nucleophiles. In kinetically controlled experiments employing pH-Stat-mode, the ester substrates Z-Ala-OMe and Z-Gly-OMe were coupled with alanine, glutamine, and Cys(Acm)-OH, respectively. Under optimized reaction conditions (pH 9.2, high ratio nucleophile/carboxyl component, 10 mumol substrate mg-1 papain), the peptide yields ranged from 17% to 79%, depending on the structure of the amino and/or carboxyl component. The peptides formed were not hydrolysed under the chosen reaction conditions. With Z-Gly-OMe as the ester substrate, formation of the dipeptide was both rapid and high yielding. Papain-catalysed formation of peptide bonds applying free amino acids as nucleophiles might serve as an economic and easily manageable approach for the synthesis of short-chain peptides to be used in clinical nutrition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids
  • Dipeptides / biosynthesis*
  • Dipeptides / chemical synthesis
  • Dipeptides / isolation & purification
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Sequence Data
  • Papain / metabolism*

Substances

  • Amino Acids
  • Dipeptides
  • Papain