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Published on: February 21, 2019
Surfactant-lactoperoxidase complex catalytically active in organic media
1Department of Chemical Systems and Engineering, Graduate School of Engineering, Kyushu University, 6-10-1, Hakozaki, Higashiku, 812-8581, Fukuoka, Japan
Biochemical Engineering Journal
|August 26, 2000
Summary
A novel surfactant-lactoperoxidase (LPO) complex shows catalytic activity in organic solvents for 2,6-dimethoxyphenol oxidation. This enzyme preparation offers enhanced stability for industrial applications.
Area of Science:
- Biocatalysis
- Enzyme Engineering
- Organic Chemistry
Background:
- Enzymes often lose activity in organic solvents.
- Developing stable, active enzyme preparations for organic media is crucial for industrial biocatalysis.
Purpose of the Study:
- To develop a catalytically active surfactant-lactoperoxidase (LPO) complex in organic solvents.
- To optimize conditions for the LPO complex's catalytic oxidation of 2,6-dimethoxyphenol (2,6-DMP).
Main Methods:
- Emulsion coating method to create a surfactant-LPO complex.
- Investigated effects of pH, oxidants (H2O2), and organic solvents on 2,6-DMP oxidation.
- Compared stability with surfactant-horseradish peroxidase complex.
Main Results:
- The surfactant-LPO complex demonstrated catalytic activity in organic solvents, unlike lyophilized LPO.
- Optimum activity was achieved with pH 8 during preparation and hydrogen peroxide as the oxidant in chloroform.
- The LPO complex exhibited superior storage stability compared to a surfactant-horseradish peroxidase complex.
Conclusions:
- A surfactant-LPO complex prepared via emulsion coating is catalytically active in organic solvents.
- Optimized conditions enhance the efficiency of 2,6-DMP oxidation.
- The superior storage stability of the LPO complex makes it promising for industrial peroxidase applications.
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