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Enhanced functionality and stabilization of a cold active laccase using nanotechnology based
Arka Mukhopadhyay1, Anjan Kr Dasgupta1, Krishanu Chakrabarti1
1Department of Biochemistry, University of Calcutta, West Bengal, India.
Bioresource Technology
|January 16, 2015
Summary
This study introduces a nanotechnology method to improve psychrophilic laccase enzyme stability and activity. Copper oxide nanoparticles and single-walled nanotubes enhance enzyme performance across a wide temperature range, enabling versatile biocatalysis.
Area of Science:
- Biotechnology
- Nanotechnology
- Enzyme Engineering
Background:
- Psychrophilic enzymes offer advantages for low-temperature biocatalysis but often lack stability.
- Enzyme immobilization is crucial for enhancing stability and reusability in industrial applications.
- Nanomaterials present novel platforms for enzyme modification and performance enhancement.
Purpose of the Study:
- To develop a nanotechnology-based immobilization technique for psychrophilic laccase.
- To enhance the psychrostability and activity of laccase using copper oxide nanoparticles and single-walled nanotubes.
- To investigate the enzyme's stability and reusability under various temperature conditions.
Main Methods:
- Immobilization of psychrophilic laccase using copper oxide nanoparticles (NP) and single-walled nanotubes (SWNT).
- Supplementation with copper (NP-laccase) as a cationic activator.
- Evaluation of enzyme activity and stability at temperatures ranging from 4°C to 80°C.
- Assessment of enzyme reusability through multiple release and re-trapping cycles.
- Testing of enzyme stability after repeated freezing and thawing cycles.
Main Results:
- Immobilization with NP and SWNT significantly enhanced laccase activity and stability at both low (4°C) and high (80°C) temperatures.
- The immobilized enzyme retained significant activity after multiple release and re-trapping cycles.
- Laccase immobilized in SWNT demonstrated stability against repeated freezing and thawing.
- The nanotechnology approach successfully imparted psychrostability and broadened the operational temperature range of the enzyme.
Conclusions:
- Nanotechnology-based immobilization using copper oxide nanoparticles and single-walled nanotubes is an effective strategy to enhance psychrophilic laccase activity and stability.
- This technique allows for enzyme operation across a wide temperature spectrum, including sub-optimal and supra-optimal conditions.
- The developed method offers a versatile platform for low-temperature biocatalysis with the potential for temperature-shift applications.
