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Updated: Jul 4, 2026
10:42
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
Published on: February 27, 2019
Continuous production of kyotorphin
A Flörsheimer1, M R Kula, H J Schütz
1Institut für Enzymtechnologie der Universität Düsseldorf, in der Kernforschungsanlage Jülich, Postfach 2050, D-5170 Jülich, FRG.
Biotechnology and Bioengineering
|May 1, 1989
Summary
Continuous peptide synthesis of kyotorphin using alpha-chymotrypsin was optimized. Soluble enzyme in a membrane reactor outperformed immobilized enzyme, showing better activity and selectivity for this enzymatic synthesis.
Area of Science:
- Biocatalysis
- Enzyme Engineering
- Peptide Synthesis
Background:
- Kyotorphin (tyrosyl-arginine) is a biologically active peptide.
- Enzymatic synthesis offers a greener alternative to chemical peptide production.
- Continuous processes are desirable for industrial scalability.
Purpose of the Study:
- To develop a continuous alpha-chymotrypsin-catalyzed synthesis of kyotorphin.
- To compare the efficacy of immobilized versus soluble enzyme systems.
- To investigate kinetic parameters and selectivity in both reaction setups.
Main Methods:
- Continuous synthesis using immobilized alpha-chymotrypsin in a packed-bed reactor.
- Continuous synthesis using soluble alpha-chymotrypsin in an enzyme membrane reactor.
- Analysis of enzyme activity, selectivity, and kinetic parameters.
Main Results:
- Soluble alpha-chymotrypsin in an enzyme membrane reactor demonstrated superior performance.
- Immobilization of alpha-chymotrypsin onto Eupergit C resulted in significant loss of activity and selectivity.
- Addition of organic solvents like n-propanol severely diminished enzyme activity.
Conclusions:
- Enzyme membrane reactors are more effective for continuous kyotorphin synthesis with alpha-chymotrypsin.
- Enzyme immobilization strategies require careful optimization to maintain activity and selectivity.
- Process conditions, including solvent use, critically impact enzyme performance in peptide synthesis.
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