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Preparation of Functional Silica Using a Bioinspired Method
Published on: August 1, 2018
Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: a simple and effective method for enzyme
Moon Il Kim1, Jungbae Kim, Jinwoo Lee
1Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Republic of Korea.
Biotechnology and Bioengineering
|September 21, 2006
Summary
Hierarchically-ordered mesocellular silica effectively immobilizes alpha-chymotrypsin and lipase, forming stable crosslinked enzyme aggregates (CLEAs). This method enhances enzyme stability and loading capacity, preventing leaching and autolysis for improved enzyme performance.
Area of Science:
- Biotechnology
- Materials Science
- Enzyme Engineering
Background:
- Enzyme immobilization is crucial for enhancing enzyme stability and reusability.
- Mesoporous silica materials offer high surface area for enzyme loading.
- Developing robust enzyme immobilization strategies remains a key challenge.
Purpose of the Study:
- To immobilize alpha-chymotrypsin (CT) and lipase (LP) using hierarchically-ordered mesocellular silica (HMMS).
- To enhance enzyme stability and prevent leaching through crosslinked enzyme aggregate (CLEA) formation within HMMS.
- To evaluate the loading capacity and activity of immobilized enzymes.
Main Methods:
- Enzyme adsorption onto HMMS followed by glutaraldehyde (GA) crosslinking to form CLEAs.
- Entrapment of CLEAs within the mesocellular pores of HMMS.
- Stability assays under shaking conditions and assessment of autolysis resistance.
- Measurement of specific activity for immobilized lipase.
Main Results:
- CLEAs of CT (CLEA-CT) and LP (CLEA-LP) were successfully formed and entrapped in HMMS.
- CLEA-CT in HMMS exhibited high enzyme loading and no activity loss for 2 weeks under shaking.
- Immobilized CT showed significantly enhanced stability compared to adsorbed CT and free CT.
- CLEA-CT in HMMS was resistant to tryptic digestion, indicating no autolysis.
- CLEA-LP in HMMS retained 30% of free lipase specific activity with greatly enhanced stability.
Conclusions:
- HMMS is an effective host material for enzyme immobilization.
- The proposed method yields highly stable and active immobilized enzymes with high loading.
- Enzyme immobilization via CLEA formation in HMMS prevents leaching and autolysis, significantly improving enzyme performance.
