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Published on: May 4, 2022
Coaggregate of trypsin and chymotrypsin
1Chemistry Department, Indian Institute of Technology, Hauz Khas, New Delhi, India.
Biotechnology and Bioengineering
|February 20, 1988
Summary
Enzyme immobilization via chemical aggregation reduces reactor size without inert carriers. This coaggregate of trypsin and chymotrypsin also shows decreased trypsin self-digestion, enhancing enzyme stability.
Area of Science:
- Biochemistry
- Enzyme Engineering
- Biotechnology
Background:
- Immobilized enzymes offer advantages in biocatalysis and industrial applications.
- Traditional immobilization often requires inert carriers, increasing reactor volume and cost.
- Enzyme self-degradation (autolysis) can limit the operational stability of enzyme preparations.
Purpose of the Study:
- To develop an enzyme immobilization method using chemical aggregation without inert carriers.
- To create a coaggregate of trypsin and chymotrypsin.
- To evaluate the stability of the immobilized enzyme preparation, specifically focusing on reduced autolysis.
Main Methods:
- Enzymes (trypsin and chymotrypsin) were chemically aggregated using glutaraldehyde cross-linking.
- The resulting coaggregate was analyzed for its physical properties and enzyme activity.
- Autolysis of the trypsin component within the coaggregate was assessed.
Main Results:
- A method for coaggregating trypsin and chymotrypsin was successfully established.
- The absence of an inert carrier allowed for a significant reduction in reactor volume.
- A notable decrease in the autolysis of the trypsin component within the coaggregate was observed.
Conclusions:
- Chemical aggregation provides an efficient method for enzyme immobilization, reducing reactor volume.
- The trypsin-chymotrypsin coaggregate exhibits enhanced stability due to reduced autolysis.
- This approach holds potential for more compact and stable biocatalytic systems.
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