Immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis

This work reviews the stripping off, role of water molecules in activity, and flexibility of immobilized Candida antarctica lipase B (CALB). Employment of CALB in ring opening polyester synthesis emphasizing on a polylactide is discussed in detail. Execution of enzymes in place of inorganic catalyst...

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Main Authors: Idris, Ani, Bukhari, Attaullah
Format: Article
Published: Elsevier Ltd. 2012
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Online Access:http://eprints.utm.my/id/eprint/47075/
http://dx.doi.org/10.1016/j.biotechadv.2011.10.002
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spelling my.utm.470752019-03-31T08:31:35Z http://eprints.utm.my/id/eprint/47075/ Immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis Idris, Ani Bukhari, Attaullah TP Chemical technology This work reviews the stripping off, role of water molecules in activity, and flexibility of immobilized Candida antarctica lipase B (CALB). Employment of CALB in ring opening polyester synthesis emphasizing on a polylactide is discussed in detail. Execution of enzymes in place of inorganic catalysts is the most green alternative for sustainable and environment friendly synthesis of products on an industrial scale. Robust immobilization and consequently performance of enzyme is the essential objective of enzyme application in industry. Water bound to the surface of an enzyme (contact class of water molecules) is inevitable for enzyme performance; it controls enzyme dynamics via flexibility changes and has intensive influence on enzyme activity. The value of pH during immobilization of CALB plays a critical role in fixing the active conformation of an enzyme. Comprehensive selection of support and protocol can develop a robust immobilized enzyme thus enhancing its performance. Organic solvents with a log P value higher than four are more suitable for enzymatic catalysis as these solvents tend to strip away very little of the enzyme surface bound water molecules. Alternatively ionic liquid can work as a more promising reaction media. Covalent immobilization is an exclusively reliable technique to circumvent the leaching of enzymes and to enhance stability. Activated polystyrene nanoparticles can prove to be a practical and economical support for chemical immobilization of CALB. In order to reduce the E-factor for the synthesis of biodegradable polymers; enzymatic ring opening polyester synthesis (eROPS) of cyclic monomers is a more sensible route for polyester synthesis. Synergies obtained from ionic liquids and immobilized enzyme can be much effective eROPS. Elsevier Ltd. 2012 Article PeerReviewed Idris, Ani and Bukhari, Attaullah (2012) Immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis. Biotechnology Advances, 30 (3). pp. 550-563. ISSN 0734-9750 http://dx.doi.org/10.1016/j.biotechadv.2011.10.002 DOI:10.1016/j.biotechadv.2011.10.002
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
topic TP Chemical technology
spellingShingle TP Chemical technology
Idris, Ani
Bukhari, Attaullah
Immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis
description This work reviews the stripping off, role of water molecules in activity, and flexibility of immobilized Candida antarctica lipase B (CALB). Employment of CALB in ring opening polyester synthesis emphasizing on a polylactide is discussed in detail. Execution of enzymes in place of inorganic catalysts is the most green alternative for sustainable and environment friendly synthesis of products on an industrial scale. Robust immobilization and consequently performance of enzyme is the essential objective of enzyme application in industry. Water bound to the surface of an enzyme (contact class of water molecules) is inevitable for enzyme performance; it controls enzyme dynamics via flexibility changes and has intensive influence on enzyme activity. The value of pH during immobilization of CALB plays a critical role in fixing the active conformation of an enzyme. Comprehensive selection of support and protocol can develop a robust immobilized enzyme thus enhancing its performance. Organic solvents with a log P value higher than four are more suitable for enzymatic catalysis as these solvents tend to strip away very little of the enzyme surface bound water molecules. Alternatively ionic liquid can work as a more promising reaction media. Covalent immobilization is an exclusively reliable technique to circumvent the leaching of enzymes and to enhance stability. Activated polystyrene nanoparticles can prove to be a practical and economical support for chemical immobilization of CALB. In order to reduce the E-factor for the synthesis of biodegradable polymers; enzymatic ring opening polyester synthesis (eROPS) of cyclic monomers is a more sensible route for polyester synthesis. Synergies obtained from ionic liquids and immobilized enzyme can be much effective eROPS.
format Article
author Idris, Ani
Bukhari, Attaullah
author_facet Idris, Ani
Bukhari, Attaullah
author_sort Idris, Ani
title Immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis
title_short Immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis
title_full Immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis
title_fullStr Immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis
title_full_unstemmed Immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis
title_sort immobilized candida antartica lipase b: hydration, stripping off and application in ring opening polyester synthesis
publisher Elsevier Ltd.
publishDate 2012
url http://eprints.utm.my/id/eprint/47075/
http://dx.doi.org/10.1016/j.biotechadv.2011.10.002
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score 13.209306