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Immobilized heparinase: In vitro reactor model.
H Bernstein1, V C Yang, R Langer
1Department of Chemical Engineering, MIT and Harvard MIT Division of Health Sciences and Technology Cambridge, Massachusetts 02139.
Biotechnology and Bioengineering
|August 5, 1987
Summary
Immobilized heparinase maintains enzyme kinetics comparable to the free enzyme, offering a viable method for preventing heparin-related complications during extracorporeal perfusions. Reactor modeling accurately predicts performance.
Area of Science:
- Biochemistry
- Chemical Engineering
- Biotechnology
Background:
- Heparinase immobilized on agarose aids in degrading heparin, preventing thromboembolic issues during extracorporeal perfusions.
- Understanding the kinetics of immobilized heparinase is crucial for optimizing its application.
Purpose of the Study:
- To investigate the kinetic properties of heparinase covalently bound to 8% agarose.
- To characterize the performance of a reactor utilizing immobilized heparinase.
Main Methods:
- Determined partition coefficient, K(m), and activation energy for immobilized heparinase.
- Assessed pH and salt concentration optima for enzyme activity.
- Modeled reactor behavior as a continuously stirred tank reactor (CSTR) using residence time distribution analysis.
Main Results:
- Immobilized heparinase exhibited kinetic parameters (K(m), activation energy) statistically similar to the free enzyme.
- Optimum pH shifted to 7.0-7.4 for immobilized enzyme, compared to 6.5 for soluble enzyme.
- Reactor model accurately predicted experimental conversions within 7-13% deviation.
Conclusions:
- Immobilized heparinase retains significant enzymatic activity and is suitable for preventing heparin-induced complications.
- The developed reactor model provides a reliable tool for predicting performance in various operational conditions.
