Studies on the catalytic performance of lignin peroxidase in nonionic reversed micelles.
- Author:
Wen-Juan ZHANG
1
;
Dan WANG
;
Xi-Rong HUANG
;
Yin-Bo QU
;
Pei-Ji GAO
Author Information
1. Key Laboratory of Colloid & Interface Chemistry of the Education Ministry of China, Shandong University, Jinan 250100, China.
- Publication Type:Journal Article
- MeSH:
Catalysis;
Cyclohexanes;
chemistry;
Enzyme Activation;
drug effects;
Micelles;
Octoxynol;
chemistry;
Pentanols;
chemistry;
Peroxidases;
metabolism;
Surface-Active Agents;
chemistry
- From:
Chinese Journal of Biotechnology
2005;21(4):654-657
- CountryChina
- Language:Chinese
-
Abstract:
Lignin peroxidase (LiP) hosted in Brij 30/cyclohexane/water nonionic reversed micelle could express its catalytic activity, but in Triton X-100/n-pentanol/cyclohexane/water nonionic reversed micelle LiP didn't show any catalytic activity. Some key factors that affected the catalytic activity of LiP in Brij 30 reversed micelle were studied at 20 degrees C. The optimum conditions were:omega0 = 8.5, pH = 2.2, [Brij30] = 600 mmol/L; under these conditions the half time of LiP was ca. 50 hours. As compared with the properties of LiP in aqueous solution, the activity of LiP hosted in Brij 30 reversed micelle dropped, but its stability improved greatly. To reveal the role of normal alcohol, which was a necessary component for forming Triton X-100 reversed micelles, the effect of n-pentanol on the catalytic activity of LiP in Brij 30 reversed micelle was investigated. Results indicated that high concentration of the alcohol deactivated LiP. So it was deduced that the phenomenon that LiP hosted in the Triton X-100 reversed micelles could not express its activity was mainly due to the alcohol co-surfactant.
