TY - JOUR
T1 - Surfactant-lactoperoxidase complex catalytically active in organic media
AU - Okazaki, Shin Ya
AU - Uchimura, Youichi
AU - Goto, Masahiro
AU - Furusaki, Shintaro
N1 - Funding Information:
This research was supported by (1) a Grant-in-Aid for Scientific Research (B) (10 555 284) from the Ministry of Education, Science, Sports and Culture of Japan, (2) Kyushu University Interdisciplinary Programs in Education and Projects in Research Development (to MG) and (3) the Proposal-Based New Industry Creative Type Technology R&D Promotion Program from the New Energy and Industrial Technology Development Organization (NEDO) of Japan (to SF and MG). SO was supported by Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists (JSPS).
PY - 2000
Y1 - 2000
N2 - A surfactant-lactoperoxidase (LPO) complex catalytically active in organic solvents was developed by the emulsion coating method. The oxidation of 2,6-dimethoxyphenol (2,6-DMP) was conducted by the surfactant-LPO complex in organic media. The LPO complex efficiently catalyzed the oxidation of 2,6-DMP in various organic solvents, although lyophilized LPO did not display the catalytic activity at all. To optimize the preparation and reaction conditions for the surfactant-LPO complex, we examined the effects of pH value in the water pools of W/O emulsions, kinds of oxidants, and the nature of organic solvents on the oxidation reaction. Its optimum activity was obtained when the pH value of the aqueous enzyme solution was adjusted to ca. 8 at the preparation stage. The LPO complex exhibited the highest catalytic activity in chloroform when H2O2 was employed as the oxidant. Furthermore, the storage stability of the surfactant-LPO complex was far better than that of the surfactant-horseradish peroxidase complex. This high storage stability of the LPO complex will be a benefit for industrial usage of peroxidases. (C) 2000 Elsevier Science S.A.
AB - A surfactant-lactoperoxidase (LPO) complex catalytically active in organic solvents was developed by the emulsion coating method. The oxidation of 2,6-dimethoxyphenol (2,6-DMP) was conducted by the surfactant-LPO complex in organic media. The LPO complex efficiently catalyzed the oxidation of 2,6-DMP in various organic solvents, although lyophilized LPO did not display the catalytic activity at all. To optimize the preparation and reaction conditions for the surfactant-LPO complex, we examined the effects of pH value in the water pools of W/O emulsions, kinds of oxidants, and the nature of organic solvents on the oxidation reaction. Its optimum activity was obtained when the pH value of the aqueous enzyme solution was adjusted to ca. 8 at the preparation stage. The LPO complex exhibited the highest catalytic activity in chloroform when H2O2 was employed as the oxidant. Furthermore, the storage stability of the surfactant-LPO complex was far better than that of the surfactant-horseradish peroxidase complex. This high storage stability of the LPO complex will be a benefit for industrial usage of peroxidases. (C) 2000 Elsevier Science S.A.
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U2 - 10.1016/S1369-703X(00)00078-4
DO - 10.1016/S1369-703X(00)00078-4
M3 - Article
AN - SCOPUS:0033823443
SN - 1369-703X
VL - 6
SP - 103
EP - 107
JO - Biochemical Engineering Journal
JF - Biochemical Engineering Journal
IS - 2
ER -