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Immobilized Candida antarctica lipase B: Hydration, stripping off and application in ring opening polyester synthesis.
Biotechnol Adv. 2012 May-Jun; 30(3):550-63.BA

Abstract

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.

Authors+Show Affiliations

Department of Bioprocess Engineering, Faculty of Chemical Engineering, Universiti Teknologi Malaysia, 81310 UTM Skudai, Johor, Malaysia. ani@cheme.utm.myNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

22041165

Citation

Idris, Ani, and Attaullah Bukhari. "Immobilized Candida Antarctica Lipase B: Hydration, Stripping Off and Application in Ring Opening Polyester Synthesis." Biotechnology Advances, vol. 30, no. 3, 2012, pp. 550-63.
Idris A, Bukhari A. Immobilized Candida antarctica lipase B: Hydration, stripping off and application in ring opening polyester synthesis. Biotechnol Adv. 2012;30(3):550-63.
Idris, A., & Bukhari, A. (2012). Immobilized Candida antarctica lipase B: Hydration, stripping off and application in ring opening polyester synthesis. Biotechnology Advances, 30(3), 550-63. https://doi.org/10.1016/j.biotechadv.2011.10.002
Idris A, Bukhari A. Immobilized Candida Antarctica Lipase B: Hydration, Stripping Off and Application in Ring Opening Polyester Synthesis. Biotechnol Adv. 2012 May-Jun;30(3):550-63. PubMed PMID: 22041165.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Immobilized Candida antarctica lipase B: Hydration, stripping off and application in ring opening polyester synthesis. AU - Idris,Ani, AU - Bukhari,Attaullah, Y1 - 2011/10/24/ PY - 2011/04/21/received PY - 2011/09/09/revised PY - 2011/10/04/accepted PY - 2011/11/2/entrez PY - 2011/11/2/pubmed PY - 2012/8/2/medline SP - 550 EP - 63 JF - Biotechnology advances JO - Biotechnol. Adv. VL - 30 IS - 3 N2 - 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. SN - 1873-1899 UR - https://www.unboundmedicine.com/medline/citation/22041165/Immobilized_Candida_antarctica_lipase_B:_Hydration_stripping_off_and_application_in_ring_opening_polyester_synthesis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0734-9750(11)00183-2 DB - PRIME DP - Unbound Medicine ER -