TY - JOUR
T1 - Catalytic properties of lignin peroxidase ALiP-P3 hosted in reversed micelles
AU - Michizoe, Junji
AU - Okazaki, Shin Ya
AU - Goto, Masahiro
AU - Furusaki, Shintaro
N1 - Funding Information:
This research was supported by (1) a Grant-in-Aid for Scientific Research (B) (10555284) 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 - 2001
Y1 - 2001
N2 - Lignin peroxidase ALiP-P3 from Actinomyces Streptomyces viridosporus T7A (ATCC 39115) became catalytically active by being entrapped in reversed micelles (RM) in an organic solvent. Streptomyces viridosporus T7A was cultivated and the culture supernatant was purified by precipitation with ammonium sulfate and finally ALiP-P3 was concentrated by ultrafiltration. Catalytic performance of lyophilized ALiP-P3 and immobilized ALiP-P3 in RM formulated with a surfactant sodium bis(2-ethylhexyl)sulphosuccinate (AOT) or n-hexadecyl trimethylammonium bromide (CTAB) was investigated by an oxidative reaction. The enzymatic activity was observed only when the enzyme was immobilized in the AOT RM. To optimize the preparation and reaction conditions for ALiP-P3 entrapped in RM, we examined the effects of pH in the water pools of RM, the degree of hydration of the surfactant (Wo), the reaction temperature and the concentration of H2O2 in the reaction medium. ALiP-P3 hosted in RM provided the highest enzymatic activity under the following conditions: pH 9.0, Wo = 20, [H2O2] = 40 mM, and 20°C. The reaction product produced by ALiP-P3 in isooctane was confirmed to be identical to that in aqueous media.
AB - Lignin peroxidase ALiP-P3 from Actinomyces Streptomyces viridosporus T7A (ATCC 39115) became catalytically active by being entrapped in reversed micelles (RM) in an organic solvent. Streptomyces viridosporus T7A was cultivated and the culture supernatant was purified by precipitation with ammonium sulfate and finally ALiP-P3 was concentrated by ultrafiltration. Catalytic performance of lyophilized ALiP-P3 and immobilized ALiP-P3 in RM formulated with a surfactant sodium bis(2-ethylhexyl)sulphosuccinate (AOT) or n-hexadecyl trimethylammonium bromide (CTAB) was investigated by an oxidative reaction. The enzymatic activity was observed only when the enzyme was immobilized in the AOT RM. To optimize the preparation and reaction conditions for ALiP-P3 entrapped in RM, we examined the effects of pH in the water pools of RM, the degree of hydration of the surfactant (Wo), the reaction temperature and the concentration of H2O2 in the reaction medium. ALiP-P3 hosted in RM provided the highest enzymatic activity under the following conditions: pH 9.0, Wo = 20, [H2O2] = 40 mM, and 20°C. The reaction product produced by ALiP-P3 in isooctane was confirmed to be identical to that in aqueous media.
UR - http://www.scopus.com/inward/record.url?scp=0034894332&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034894332&partnerID=8YFLogxK
U2 - 10.1016/S1369-703X(01)00093-6
DO - 10.1016/S1369-703X(01)00093-6
M3 - Article
AN - SCOPUS:0034894332
SN - 1369-703X
VL - 8
SP - 129
EP - 134
JO - Biochemical Engineering Journal
JF - Biochemical Engineering Journal
IS - 2
ER -