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A SiO2 Microcarrier with an Opal-like Structure for Cross-Linked Enzyme Immobilization
Yixian Luo1, Dou Jin1, Wenjin He2
1Engineering Research Center of Industrial Microbiology of Ministry of Education, College of Life Sciences, Fujian Normal University, Fuzhou, Fujian 350117, China.
Langmuir : the ACS Journal of Surfaces and Colloids
|November 18, 2021
Summary
Opal-like silica microcarriers were developed for enzyme immobilization. Neopentyl glycol diglycidyl ether (NGDE) enhanced enzyme activity and stability for Rhizopus oryzae lipase (ROL) and Aspergillus oryzae α-amylases (AOA) immobilization.
Area of Science:
- Materials Science
- Biotechnology
- Chemical Engineering
Background:
- Enzyme immobilization is crucial for industrial applications, requiring stable and efficient carrier materials.
- Opal-like silica (SiO2) microcarriers offer unique structural properties for biomolecule support.
- Developing novel cross-linking agents can improve enzyme stability and activity upon immobilization.
Purpose of the Study:
- To synthesize and characterize opal-like SiO2 microcarriers (opal-SiO2I and opal-SiO2II) with varying pore sizes.
- To immobilize Rhizopus oryzae lipase (ROL) and Aspergillus oryzae α-amylases (AOA) onto these microcarriers using neopentyl glycol diglycidyl ether (NGDE) as a cross-linking agent.
- To evaluate the impact of NGDE cross-linking and microcarrier properties on enzyme performance, stability, and reusability.
Main Methods:
- Synthesis of SiO2 microcarriers with opal-like structures and different pore diameters.
- Enzyme immobilization of ROL and AOA using NGDE as a cross-linking agent, comparing its efficacy to glutaraldehyde.
- Morphological analysis using electron microscopy to assess microcarrier structure and enzyme distribution.
- Enzyme activity assays, pH and thermal stability tests, and reusability experiments to quantify enzyme performance.
Main Results:
- Opal-like SiO2 microcarriers with distinct pore sizes were successfully synthesized.
- NGDE proved effective as a cross-linking agent, enabling stable enzyme immobilization.
- Enzymes immobilized on opal-SiO2II, possessing a larger specific surface area, exhibited superior performance compared to opal-SiO2I.
- Immobilized ROL and AOA (ROL@opal-SiO2II and AOA@opal-SiO2II) showed significantly enhanced activity (5.32 and 9.32 times, respectively) compared to free enzymes.
- Improved pH and thermal stability, along with enhanced reusability, were observed for enzymes immobilized on opal-SiO2II.
Conclusions:
- Opal-like SiO2 microcarriers, particularly opal-SiO2II, are effective supports for enzyme immobilization.
- NGDE is a promising cross-linking agent for enhancing enzyme activity, stability, and reusability.
- The developed immobilized enzyme systems demonstrate significant potential for industrial applications requiring efficient biocatalysis.
