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In Situ Calb Enzyme Immobilization in Mesoporous Material Type MCM-48 Synthesis Using Ionic Solid [C14MI]Cl as
Catia S Zanchett Battiston1,2, Aline M Moreira Ficanha2,3, Carolina E Demaman Oro2
1IFRS - Erechim, Erechim, RS, 99713-028, Brazil.
Applied Biochemistry and Biotechnology
|September 15, 2021
Summary
A novel MCM-48 mesoporous support was developed for immobilizing Candida antarctica B (CALB) enzyme. This optimized support demonstrates high esterification activity and stability, offering industrial potential for enzyme applications.
Area of Science:
- Materials Science
- Biotechnology
- Chemical Engineering
Background:
- Enzyme immobilization is crucial for industrial biocatalysis, enhancing stability and reusability.
- Mesoporous materials offer high surface area and tunable pore structures for effective enzyme loading.
- Candida antarctica B (CALB) is a widely used lipase for esterification reactions.
Purpose of the Study:
- To synthesize and characterize a novel MCM-48 mesoporous support using 1-tetradecyl-3-methylimidazolium chloride ([C14MI]Cl) as a structure-directing agent.
- To achieve in situ immobilization of Candida antarctica B (CALB) onto the synthesized MCM-48 support.
- To optimize the immobilization conditions and evaluate the esterification activity, stability, and reusability of the CALB-MCM-48 biocatalyst.
Main Methods:
- Synthesis of MCM-48 mesoporous support using [C14MI]Cl.
- In situ immobilization of CALB enzyme onto the MCM-48 support.
- Characterization of support porosity (pore size, specific area, pore volume).
- Optimization of immobilization parameters using a mathematical model.
- Assay of esterification activity and yield.
- Evaluation of thermal and storage stability, and reusability.
Main Results:
- The MCM-48[C14MI]Cl support exhibited mesoporous characteristics with significant pore size increase upon enzyme immobilization.
- Optimized conditions (0.31 g enzyme, 3.35% ionic solid) yielded maximum esterification activity of 392.92 U/g and 688% yield.
- The immobilized enzyme retained over 50% activity after 75 days of refrigeration.
- High residual activity was observed at elevated temperatures (80% at 60°C, 40% at 80°C).
- The biocatalyst demonstrated reusability for up to 10 cycles with approximately 50% residual activity.
Conclusions:
- The synthesized MCM-48 mesoporous support effectively facilitates in situ immobilization of CALB.
- The optimized CALB-MCM-48 biocatalyst exhibits excellent esterification activity, stability, and reusability.
- This novel biocatalyst holds significant promise for industrial applications in esterification processes.
