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Published on: March 29, 2018
Stem bromelain: an enzyme that naturally facilitates oriented immobilization
Hafeeza Khatoon1, Hina Younus, Mohammad Saleemuddin
1Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India.
Protein and Peptide Letters
|March 10, 2007
Summary
Immobilizing stem bromelain using periodic acid oxidation and amino-Sepharose coupling creates a uniformly oriented enzyme. This preparation shows enhanced proteolytic activity and thermal stability compared to other methods.
Area of Science:
- Biochemistry
- Enzyme immobilization
- Protein chemistry
Background:
- Stem bromelain is a cysteine protease with therapeutic and industrial applications.
- Enzyme immobilization is crucial for enhancing stability and reusability.
- Uniform orientation of immobilized enzymes can optimize activity.
Purpose of the Study:
- To develop a novel method for immobilizing stem bromelain with uniform orientation.
- To evaluate the proteolytic activity and thermal stability of the immobilized enzyme.
Main Methods:
- Stem bromelain's oligosaccharide chain was oxidized using periodic acid to introduce aldehyde groups.
- The oxidized enzyme was coupled to amino-Sepharose for immobilization.
- Proteolytic activity and thermal stability were compared to soluble bromelain and CNBr-activated Sepharose-immobilized bromelain.
Main Results:
- The immobilized bromelain preparation exhibited high proteolytic activity.
- Remarkably enhanced thermal stability was observed in the immobilized bromelain compared to soluble and CNBr-activated forms.
- Uniform orientation was achieved through the specific coupling method.
Conclusions:
- Periodic acid oxidation followed by coupling to amino-Sepharose is an effective method for creating uniformly oriented and highly stable immobilized stem bromelain.
- This immobilization strategy significantly improves enzyme performance for potential applications.
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