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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Main Authors: Ying Chen, Yi Xu, Xiao-mei Wu
Format: Article
Language:English
Published: Bulgarian Academy of Sciences 2015-09-01
Series:International Journal Bioautomation
Subjects:
Online Access:http://www.biomed.bas.bg/bioautomation/2015/vol_19.3/files/19.3_05.pdf
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spelling 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
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