A two‐step enzymatic synthesis of dipeptides
- 20 January 1992
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 39 (2), 132-140
- https://doi.org/10.1002/bit.260390203
Abstract
A simple system is introduced to produce dipeptides continuously by enzyme catalyzed condensation of amino acid esters and amino acid amides. Synthesis of N-terminal free dipeptide-amides is achieved by means of carboxypeptidase Y. The peptide-amide is deamidated utilizing a newly isolated peptide-amide is deamidated utilizing a newly isolated peptide-amidase. Separation of substrates and products is accomplished by anion-exchange chromatography. Modeling of the reactions shows that the two reactions have to be carried out in a cascade of two reactors in order to prevent hydrolysis of the peptide by the carboxypeptidase. Continuous production of Kyotorphin (H-TyrArg-OH) with a space–time yield of 257 g/L · d shows the feasibility of this concept.Keywords
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