TY - JOUR
T1 - Immobilization of Burkholderia sp. lipase on a ferric silica nanocomposite for biodiesel production
AU - Tran, Dang Thuan
AU - Chen, Ching Lung
AU - Chang, Jo Shu
N1 - Funding Information:
This study was financially supported by the Research Grant NSC100-3113-E-006-016- , NSC100-2218-E-126-002- , NSC101-3113-E-006-015- , and NSC99-2221-E-006-137-MY3 from Taiwan's National Science Council . The support from “Top University Grants” of National Cheng Kung University is also appreciated.
Copyright:
Copyright 2012 Elsevier B.V., All rights reserved.
PY - 2012/4/15
Y1 - 2012/4/15
N2 - In this work, lipase produced from an isolated strain Burkholderia sp. C20 was immobilized on magnetic nanoparticles to catalyze biodiesel synthesis. Core-shell nanoparticles were synthesized by coating Fe 3O 4 core with silica shell. The nanoparticles treated with dimethyl octadecyl [3-(trimethoxysilyl) propyl] ammonium chloride were used as immobilization supporters. The Burkholderia lipase was then bound to the synthesized nanoparticles for immobilization. The protein binding efficiency on alkyl-functionalized Fe 3O 4-SiO 2 was estimated as 97%, while the efficiency was only 76% on non-modified Fe 3O 4-SiO 2. Maximum adsorption capacity of lipase on alkyl-functionalized Fe 3O 4-SiO 2 was estimated as 29.45mgg -1 based on Langmuir isotherm. The hydrolytic kinetics (using olive oil as substrate) of the lipase immobilized on alkyl-grafted Fe 3O 4-SiO 2 followed Michaelis-Menten model with a maximum reaction rate and a Michaelis constant of 6251Ug -1 and 3.65mM, respectively. Physical and chemical properties of the nanoparticles and the immobilized lipase were characterized by Brunauer-Emmett-Teller (BET) analysis, scanning electron microscope (SEM), and Fourier transform infrared spectroscopy (FT-IR). Moreover, the immobilized lipase was used to catalyze the transesterification of olive oil with methanol to produce fatty acid methyl esters (FAMEs), attaining a FAMEs conversion of over 90% within 30h in batch operation when 11wt% immobilized lipase was employed. The immobilized lipase could be used for ten cycles without significant loss in its transesterification activity.
AB - In this work, lipase produced from an isolated strain Burkholderia sp. C20 was immobilized on magnetic nanoparticles to catalyze biodiesel synthesis. Core-shell nanoparticles were synthesized by coating Fe 3O 4 core with silica shell. The nanoparticles treated with dimethyl octadecyl [3-(trimethoxysilyl) propyl] ammonium chloride were used as immobilization supporters. The Burkholderia lipase was then bound to the synthesized nanoparticles for immobilization. The protein binding efficiency on alkyl-functionalized Fe 3O 4-SiO 2 was estimated as 97%, while the efficiency was only 76% on non-modified Fe 3O 4-SiO 2. Maximum adsorption capacity of lipase on alkyl-functionalized Fe 3O 4-SiO 2 was estimated as 29.45mgg -1 based on Langmuir isotherm. The hydrolytic kinetics (using olive oil as substrate) of the lipase immobilized on alkyl-grafted Fe 3O 4-SiO 2 followed Michaelis-Menten model with a maximum reaction rate and a Michaelis constant of 6251Ug -1 and 3.65mM, respectively. Physical and chemical properties of the nanoparticles and the immobilized lipase were characterized by Brunauer-Emmett-Teller (BET) analysis, scanning electron microscope (SEM), and Fourier transform infrared spectroscopy (FT-IR). Moreover, the immobilized lipase was used to catalyze the transesterification of olive oil with methanol to produce fatty acid methyl esters (FAMEs), attaining a FAMEs conversion of over 90% within 30h in batch operation when 11wt% immobilized lipase was employed. The immobilized lipase could be used for ten cycles without significant loss in its transesterification activity.
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U2 - 10.1016/j.jbiotec.2012.01.018
DO - 10.1016/j.jbiotec.2012.01.018
M3 - Article
C2 - 22306108
AN - SCOPUS:84862817808
SN - 0168-1656
VL - 158
SP - 112
EP - 119
JO - Journal of Biotechnology
JF - Journal of Biotechnology
IS - 3
ER -