TY - JOUR
T1 - Highly active lipase immobilized on biogenous iron oxide via an organic bridging group
T2 - The dramatic effect of the immobilization support on enzymatic function
AU - Ema, Tadashi
AU - Miyazaki, Yuki
AU - Kozuki, Izumi
AU - Sakai, Takashi
AU - Hashimoto, Hideki
AU - Takada, Jun
PY - 2011/11
Y1 - 2011/11
N2 - Iron-oxidizing bacteria, Leptothrix ochracea, produce biogenous iron oxide (BIO), while the heat treatment of BIO gives its magnetized material (m-BIO). In this study, they were chemically modified with silane coupling agents to give organic-inorganic hybrid materials, which were then used as immobilization supports for enzymes. BIO-M, which was prepared by modifying BIO with 3-methacryloxypropyltrimethoxysilane, was found to be the best immobilization support. The immobilized lipases showed remarkably high catalytic activity; for example, Burkholderia cepacia lipase (BCL) immobilized on BIO-M showed a turnover frequency of 33000 h-1 for 1-phenylethanol (1a). m-BIO-M, which was prepared by modifying m-BIO with 3-methacryloxypropyltrimethoxysilane, was also used as an immobilization support. Although the lipases immobilized on m-BIO-M showed lower catalytic activity than those immobilized on BIO-M, the former could be separated and reused easily by using a magnet. These immobilized enzymes could be recycled at least five times and are environmentally benign biocatalysts.
AB - Iron-oxidizing bacteria, Leptothrix ochracea, produce biogenous iron oxide (BIO), while the heat treatment of BIO gives its magnetized material (m-BIO). In this study, they were chemically modified with silane coupling agents to give organic-inorganic hybrid materials, which were then used as immobilization supports for enzymes. BIO-M, which was prepared by modifying BIO with 3-methacryloxypropyltrimethoxysilane, was found to be the best immobilization support. The immobilized lipases showed remarkably high catalytic activity; for example, Burkholderia cepacia lipase (BCL) immobilized on BIO-M showed a turnover frequency of 33000 h-1 for 1-phenylethanol (1a). m-BIO-M, which was prepared by modifying m-BIO with 3-methacryloxypropyltrimethoxysilane, was also used as an immobilization support. Although the lipases immobilized on m-BIO-M showed lower catalytic activity than those immobilized on BIO-M, the former could be separated and reused easily by using a magnet. These immobilized enzymes could be recycled at least five times and are environmentally benign biocatalysts.
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U2 - 10.1039/c1gc15877e
DO - 10.1039/c1gc15877e
M3 - Article
AN - SCOPUS:80455163305
SN - 1463-9262
VL - 13
SP - 3187
EP - 3195
JO - Green Chemistry
JF - Green Chemistry
IS - 11
ER -