TY - JOUR
T1 - Catalytic activity of Laccase hosted in reversed micelles
AU - Michizoe, Junji
AU - Goto, Masahiro
AU - Furusaki, Shintaro
N1 - Funding Information:
We are gratefult o Daiwa Co., Ltd. for generouslyp rovidinglac-case. This researchw as supportedb y a Grant-in-Aid for Scientific Research( B) (12450322f)r om the Ministry of Education,C ulture, Sports,S ciencea ndT echnologyo f Japan,K yushuU niversityI nterdis-ciplinary Programsi n Educationa nd Projects in ResearchD evelop-ment( to M.G.) and the Proposal-BasedN ew IndustryC reativeT ype TechnologyR &D PromotionP rogramf rom the New Energy and In-dustrialT echnologyD evelopmenOt rganization(N EDO) of Japan (to M.G. andS .F.).
PY - 2001
Y1 - 2001
N2 - Nanostructured reversed micelles induce a high laccase activity in organic solvents, because enzymes can maintain their highly dimensional structure in water pools of reversed micelles [RMs]. Laccase attracts considerable attention as a novel industrial enzyme due to its high capability to catalyze the oxidation of aromatic compounds. The catalytic activities of lyophilized laccase and laccase entrapped in RMs were compared using an oxidative reaction. Laccase hosted in an anionic RM effectively catalyzed the oxidative reaction in various organic solvents, while lyophilized laccase exhibited no such catalytic activity. To optimize the Preparation and reaction conditions for laccase in RMs, we examined the effects of pH of water pools of RMs, the concentrations of both enzyme and surfactant for the preparation of RMs, the hydration ratio (Wo), and the reaction temperature on laccase catalytic activity in organic media. Laccase entrapped in RMs exhibited the highest catalytic activity in isooctane under the following conditions: bis-2-ethylhexyl sulfosuccinate sodium salt (AOT) of 100 mM, pH 6.0, Wo=40, and reaction temperature of 60°C. Under the optimum conditions, environmental pollutants such as bisphenol A, 2,4-dichlorophenol and 2,4,6-trichlorophenol were effectively degraded in 3 h.
AB - Nanostructured reversed micelles induce a high laccase activity in organic solvents, because enzymes can maintain their highly dimensional structure in water pools of reversed micelles [RMs]. Laccase attracts considerable attention as a novel industrial enzyme due to its high capability to catalyze the oxidation of aromatic compounds. The catalytic activities of lyophilized laccase and laccase entrapped in RMs were compared using an oxidative reaction. Laccase hosted in an anionic RM effectively catalyzed the oxidative reaction in various organic solvents, while lyophilized laccase exhibited no such catalytic activity. To optimize the Preparation and reaction conditions for laccase in RMs, we examined the effects of pH of water pools of RMs, the concentrations of both enzyme and surfactant for the preparation of RMs, the hydration ratio (Wo), and the reaction temperature on laccase catalytic activity in organic media. Laccase entrapped in RMs exhibited the highest catalytic activity in isooctane under the following conditions: bis-2-ethylhexyl sulfosuccinate sodium salt (AOT) of 100 mM, pH 6.0, Wo=40, and reaction temperature of 60°C. Under the optimum conditions, environmental pollutants such as bisphenol A, 2,4-dichlorophenol and 2,4,6-trichlorophenol were effectively degraded in 3 h.
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U2 - 10.1263/jbb.92.67
DO - 10.1263/jbb.92.67
M3 - Article
C2 - 16233060
AN - SCOPUS:0034889078
SN - 1389-1723
VL - 92
SP - 67
EP - 71
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
IS - 1
ER -