Efficient Improving the Activity and Enantioselectivity of Candida rugosa Lipase for the Resolution of Naproxen by Enzyme Immobilization on MCM-41 Mesoporous Molecular Sieve
Lipase from Candida rogusa was immobilized on MCM-41 mesoporous molecular sieves in a trapped aqueous-organic biphase system for the resolution of racemic naproxen methyl ester. It was interesting that the activity and enantioselectivity of the immobilized lipase were improved significantly relative...
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Bulgarian Academy of Sciences
2015-09-01
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doaj-c52870825f104bf1a40d6ee25d813d4b2020-11-25T03:29:34ZengBulgarian Academy of SciencesInternational Journal Bioautomation1314-19021314-23212015-09-01193325334Efficient Improving the Activity and Enantioselectivity of Candida rugosa Lipase for the Resolution of Naproxen by Enzyme Immobilization on MCM-41 Mesoporous Molecular SieveYing Chen0Yi XuXiao-mei WuSchool of Chemical and Environmental Engineering, Shanghai Institute of Technology, 100, Hai Quan Road, Shanghai, China, 201418Lipase from Candida rogusa was immobilized on MCM-41 mesoporous molecular sieves in a trapped aqueous-organic biphase system for the resolution of racemic naproxen methyl ester. It was interesting that the activity and enantioselectivity of the immobilized lipase were improved significantly relative to the free enzyme. The proportion of water (ml)/support (g) has a dramatic influence on the activity and enantioselectivity of lipase immobilized onto MCM-41 molecular sieves. It was also found that the activity of immobilized lipase was more sensitive to pH value and temperature than the free one. Higher pH value will increase the activity but decrease the enantioselectivity of the immobilized lipase. The enantioselectivity of the immobilized lipase was not altered significantly within the range of tested temperature. The immobilized lipase can be reused for at least 8 batches without significant lose of activity with the aid of methanotrophic bacteria to eliminate the methanol produced during the resolution process.http://www.biomed.bas.bg/bioautomation/2015/vol_19.3/files/19.3_05.pdfMCM-41ImmobilizationLipaseEnantioselectivityNaproxenStability |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ying Chen Yi Xu Xiao-mei Wu |
spellingShingle |
Ying Chen Yi Xu Xiao-mei Wu Efficient Improving the Activity and Enantioselectivity of Candida rugosa Lipase for the Resolution of Naproxen by Enzyme Immobilization on MCM-41 Mesoporous Molecular Sieve International Journal Bioautomation MCM-41 Immobilization Lipase Enantioselectivity Naproxen Stability |
author_facet |
Ying Chen Yi Xu Xiao-mei Wu |
author_sort |
Ying Chen |
title |
Efficient Improving the Activity and Enantioselectivity of Candida rugosa Lipase for the Resolution of Naproxen by Enzyme Immobilization on MCM-41 Mesoporous Molecular Sieve |
title_short |
Efficient Improving the Activity and Enantioselectivity of Candida rugosa Lipase for the Resolution of Naproxen by Enzyme Immobilization on MCM-41 Mesoporous Molecular Sieve |
title_full |
Efficient Improving the Activity and Enantioselectivity of Candida rugosa Lipase for the Resolution of Naproxen by Enzyme Immobilization on MCM-41 Mesoporous Molecular Sieve |
title_fullStr |
Efficient Improving the Activity and Enantioselectivity of Candida rugosa Lipase for the Resolution of Naproxen by Enzyme Immobilization on MCM-41 Mesoporous Molecular Sieve |
title_full_unstemmed |
Efficient Improving the Activity and Enantioselectivity of Candida rugosa Lipase for the Resolution of Naproxen by Enzyme Immobilization on MCM-41 Mesoporous Molecular Sieve |
title_sort |
efficient improving the activity and enantioselectivity of candida rugosa lipase for the resolution of naproxen by enzyme immobilization on mcm-41 mesoporous molecular sieve |
publisher |
Bulgarian Academy of Sciences |
series |
International Journal Bioautomation |
issn |
1314-1902 1314-2321 |
publishDate |
2015-09-01 |
description |
Lipase from Candida rogusa was immobilized on MCM-41 mesoporous molecular sieves in a trapped aqueous-organic biphase system for the resolution of racemic naproxen methyl ester. It was interesting that the activity and enantioselectivity of the immobilized lipase were improved significantly relative to the free enzyme. The proportion of water (ml)/support (g) has a dramatic influence on the activity and enantioselectivity of lipase immobilized onto MCM-41 molecular sieves. It was also found that the activity of immobilized lipase was more sensitive to pH value and temperature than the free one. Higher pH value will increase the activity but decrease the enantioselectivity of the immobilized lipase. The enantioselectivity of the immobilized lipase was not altered significantly within the range of tested temperature. The immobilized lipase can be reused for at least 8 batches without significant lose of activity with the aid of methanotrophic bacteria to eliminate the methanol produced during the resolution process. |
topic |
MCM-41 Immobilization Lipase Enantioselectivity Naproxen Stability |
url |
http://www.biomed.bas.bg/bioautomation/2015/vol_19.3/files/19.3_05.pdf |
work_keys_str_mv |
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