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Dipeptide synthesis and separation in a reversed micellar membrane reactor
M L Serralheiro1, D M Prazeres, J M Cabral
1Laboratório de Engenharia Bioquímica, Instituto Superior Técnico, Lisboa, Portugal.
Enzyme and Microbial Technology
|December 1, 1994
Summary
Enzyme-catalyzed dipeptide synthesis using alpha-chymotrypsin in reversed micelles was optimized. Selective precipitation integrated product separation within the membrane reactor, maintaining stable operation.
Area of Science:
- Biocatalysis
- Chemical Engineering
- Separation Technology
Background:
- Enzyme catalysis offers high specificity for synthesizing complex molecules.
- Reversed micelles provide microenvironments for enzyme stabilization and activity.
- Integrated reaction and separation processes enhance efficiency.
Purpose of the Study:
- To optimize conditions for dipeptide AcPheLeuNH2 synthesis using alpha-chymotrypsin in reversed micelles.
- To investigate the integration of product separation via selective precipitation within a membrane reactor.
- To evaluate the system's kinetics, mass transfer, and performance under batch and continuous operation.
Main Methods:
- Utilized a tubular ceramic membrane reactor operated in batch mode.
- Employed a factorial design to optimize reaction medium conditions (TTAB concentration, buffer molarity, pH).
- Investigated the influence of enzyme, surfactant (TTAB), and water concentrations on system performance.
Main Results:
- Maximum synthesis rates were achieved through optimized reaction conditions.
- Selective precipitation of the dipeptide product enabled complete retention by the ultrafiltration membrane.
- Constant permeation flow rates were maintained despite continuous solid accumulation.
Conclusions:
- Integrated biotransformation and separation were successfully demonstrated in a membrane reactor.
- The system allows for efficient dipeptide synthesis and simultaneous product recovery.
- The optimized process shows potential for continuous operation in biocatalytic synthesis.