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Interfacial behavior of Lactate Oxidase at Air-Subphase interface
Marystela Ferreira1, Shiv K Sharma2, Suraj Paudyal2
1Department of Mathematic, Physical, Chemistry, Federal University of São Paulo, Sorocaba, São Paulo, 18052-720, Brazil.
Journal of Colloid and Interface Science
|January 18, 2021
Summary
Lactate oxidase (LacOx) enzyme forms a stable, active monolayer at the air-subphase interface. Surface chemistry and spectroscopy confirm its structural integrity and prolonged activity.
Area of Science:
- Biochemistry
- Surface Chemistry
- Enzyme Kinetics
Background:
- Enzyme monolayers at interfaces are crucial for biosensors and biocatalysis.
- Understanding the surface properties of enzymes like lactate oxidase (LacOx) is key to their application.
Purpose of the Study:
- To investigate the surface chemistry and stability of a lactate oxidase (LacOx) enzyme monolayer.
- To determine the structural conformation and activity of LacOx in a monolayer format.
Main Methods:
- Surface pressure-area isotherm measurements to assess monolayer packing and stability.
- Compression-decompression cycles to evaluate monolayer resilience.
- Spectroscopic techniques including UV-vis absorption, fluorescence, and circular dichroism (CD) to analyze enzyme structure and conformation.
Main Results:
- LacOx forms a stable monolayer at the air-subphase interface without aggregation.
- The enzyme maintains activity over extended periods in the monolayer form.
- Circular dichroism (CD) spectra indicate the preservation of an alpha-helix secondary structure conformation.
Conclusions:
- Lactate oxidase (LacOx) exhibits remarkable stability and activity when confined to a monolayer at the air-subphase interface.
- The findings support the potential of LacOx monolayers in various biochemical applications requiring stable enzyme structures.
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