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Improved performance of lipases immobilized on heterofunctional octyl-glyoxyl agarose beads
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0290(19980605)58:5<486::aid-bit4>3.0.co;2-9openalex-snapshot
A single step purification, immobilization, and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports
inferredcites →https://doi.org/10.1002/adsc.201100163openalex-snapshot
Coupling Chemical Modification and Immobilization to Improve the Catalytic Performance of Enzymes
inferredcites →https://doi.org/10.1002/adsc.201100534openalex-snapshot
Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance
inferredcites →https://doi.org/10.1002/bit.21230openalex-snapshot
Improved catalytic properties of immobilized lipases by the presence of very low concentrations of detergents in the reaction medium
inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot
A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
inferredcites →https://doi.org/10.1006/jmbi.1994.1035openalex-snapshot
Crystallization and Preliminary X-ray Studies of Lipase B from Candida antarctica
inferredcites →https://doi.org/10.1007/s00253-006-0775-xopenalex-snapshot
Phospholipases and their industrial applications
inferredcites →https://doi.org/10.1007/s11746-010-1727-2openalex-snapshot
Cross‐Linking of Lipases Adsorbed on Hydrophobic Supports: Highly Selective Hydrolysis of Fish Oil Catalyzed by RML
inferredcites →https://doi.org/10.1016/0141-0229(88)90018-xopenalex-snapshot
Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes
inferredcites →https://doi.org/10.1016/0141-0229(89)90019-7openalex-snapshot
Immobilization-stabilization of enzymes; variables that control the intensity of the trypsin (amine)-agarose (aldehyde) multipoint attachment
inferredcites →https://doi.org/10.1016/0141-0229(93)90016-uopenalex-snapshot
Preparation of activated supports containing low pK amino groups. A new tool for protein immobilization via the carboxyl coupling method
inferredcites →https://doi.org/10.1016/b978-0-12-746208-0.50001-3openalex-snapshot
Methods in Carbohydrate Chemistry
inferredcites →https://doi.org/10.1016/j.biotechadv.2010.05.012openalex-snapshot
Biodiesel production with immobilized lipase: A review
inferredcites →https://doi.org/10.1016/j.biotechadv.2013.08.006openalex-snapshot
Advances in lipase-catalyzed esterification reactions
inferredcites →https://doi.org/10.1016/j.biotechadv.2014.04.011openalex-snapshot
Chemoenzymatic synthesis of polymeric materials using lipases as catalysts: A review
inferredcites →https://doi.org/10.1016/j.enzmictec.2005.03.020openalex-snapshot
Some special features of glyoxyl supports to immobilize proteins
inferredcites →https://doi.org/10.1016/j.enzmictec.2005.03.027openalex-snapshot
Immobilization of different protein fractions from Rhizomucor miehei lipase crude extract
inferredcites →https://doi.org/10.1016/j.enzmictec.2005.08.034openalex-snapshot
Glyoxyl agarose as a new chromatographic matrix
inferredcites →https://doi.org/10.1016/j.enzmictec.2005.10.014openalex-snapshot
Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins
inferredcites →https://doi.org/10.1016/j.enzmictec.2006.08.023openalex-snapshot
Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: Correlation between enzyme–support linkages and thermal stability
inferredcites →https://doi.org/10.1016/j.enzmictec.2007.01.018openalex-snapshot
Improvement of enzyme activity, stability and selectivity via immobilization techniques
inferredcites →https://doi.org/10.1016/j.enzmictec.2007.05.004openalex-snapshot
Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports
inferredcites →https://doi.org/10.1016/j.enzmictec.2009.02.009openalex-snapshot
Positive effects of the multipoint covalent immobilization in the reactivation of partially inactivated derivatives of lipase from Thermomyces lanuginosus
inferredcites →https://doi.org/10.1016/j.enzmictec.2009.08.009openalex-snapshot
Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation
inferredcites →https://doi.org/10.1016/j.enzmictec.2009.09.001openalex-snapshot
The presence of thiolated compounds allows the immobilization of enzymes on glyoxyl agarose at mild pH values: New strategies of stabilization by multipoint covalent attachment
inferredcites →https://doi.org/10.1016/j.enzmictec.2010.10.003openalex-snapshot
Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance
inferredcites →https://doi.org/10.1016/j.jbiotec.2004.09.015openalex-snapshot
Improved stabilization of chemically aminated enzymes via multipoint covalent attachment on glyoxyl supports
inferredcites →https://doi.org/10.1016/j.molcatb.2006.01.034openalex-snapshot
Immobilization of lipases for non-aqueous synthesis
inferredcites →https://doi.org/10.1016/j.molcatb.2006.02.010openalex-snapshot
Lipases: Useful biocatalysts for the preparation of pharmaceuticals
inferredcites →https://doi.org/10.1016/j.molcatb.2009.11.010openalex-snapshot
Lipase from Thermomyces lanuginosus: Uses and prospects as an industrial biocatalyst
inferredcites →https://doi.org/10.1016/j.molcatb.2010.02.003openalex-snapshot
Lipase from Rhizomucor miehei as an industrial biocatalyst in chemical process
inferredcites →https://doi.org/10.1016/j.molcatb.2010.03.008openalex-snapshot
Lipase from Rhizomucor miehei as a biocatalyst in fats and oils modification
inferredcites →https://doi.org/10.1016/j.molcatb.2014.03.005openalex-snapshot
Enantioselective resolution of racemic ibuprofen esters using different lipases immobilized on octyl sepharose
inferredcites →https://doi.org/10.1016/j.procbio.2009.02.001openalex-snapshot
Reactivation of covalently immobilized lipase from Thermomyces lanuginosus
inferredcites →https://doi.org/10.1016/j.procbio.2009.03.012openalex-snapshot
The co-operative effect of physical and covalent protein adsorption on heterofunctional supports
inferredcites →https://doi.org/10.1016/j.procbio.2009.04.015openalex-snapshot
Immobilization–stabilization of the lipase from Thermomyces lanuginosus: Critical role of chemical amination
inferredcites →https://doi.org/10.1016/j.procbio.2011.07.021openalex-snapshot
Lipase mediated synthesis of sugar fatty acid esters
inferredcites →https://doi.org/10.1016/j.procbio.2012.01.011openalex-snapshot
Lipase promiscuity and its biochemical applications
inferredcites →https://doi.org/10.1016/j.procbio.2012.02.009openalex-snapshot
The slow-down of the CALB immobilization rate permits to control the inter and intra molecular modification produced by glutaraldehyde
inferredcites →https://doi.org/10.1016/j.procbio.2012.02.026openalex-snapshot
Modulation of the properties of immobilized CALB by chemical modification with 2,3,4-trinitrobenzenesulfonate or ethylendiamine. Advantages of using adsorbed lipases on hydrophobic supports
inferredcites →https://doi.org/10.1016/j.procbio.2014.01.028openalex-snapshot
Tuning of Lecitase features via solid-phase chemical modification: Effect of the immobilization protocol
inferredcites →https://doi.org/10.1016/s0009-3084(98)00042-5openalex-snapshot
Immobilization of lipases by selective adsorption on hydrophobic supports
inferredcites →https://doi.org/10.1016/s0040-4020(03)00876-7openalex-snapshot
Regio-selective deprotection of peracetylated sugars via lipase hydrolysis
inferredcites →https://doi.org/10.1016/s0167-7799(03)00008-8openalex-snapshot
Biocatalytic transformations in ionic liquids
inferredcites →https://doi.org/10.1016/s0167-7799(96)10064-0openalex-snapshot
‘Interfacial activation’ of lipases: facts and artifacts
inferredcites →https://doi.org/10.1016/s0969-2126(00)00031-9openalex-snapshot
The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
inferredcites →https://doi.org/10.1016/s1367-5931(02)00297-1openalex-snapshot
Lipases as practical biocatalysts
inferredcites →https://doi.org/10.1016/s1381-1177(00)00168-5openalex-snapshot
Enantioselective enzymatic hydrolysis of racemic glycidyl esters by using immobilized porcine pancreas lipase with improved catalytic properties
inferredcites →https://doi.org/10.1021/bi00120a034openalex-snapshot
Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase
inferredcites →https://doi.org/10.1021/bm020071lopenalex-snapshot
Solid-Phase Handling of Hydrophobins: Immobilized Hydrophobins as a New Tool To Study Lipases
inferredcites →https://doi.org/10.1021/bm025729+openalex-snapshot
General Trend of Lipase to Self-Assemble Giving Bimolecular Aggregates Greatly Modifies the Enzyme Functionality
inferredcites →https://doi.org/10.1021/bm400762hopenalex-snapshot
Heterofunctional Supports in Enzyme Immobilization: From Traditional Immobilization Protocols to Opportunities in Tuning Enzyme Properties
inferredcites →https://doi.org/10.1021/bm800609gopenalex-snapshot
Solid-Phase Chemical Amination of a Lipase from Bacillus thermocatenulatus To Improve Its Stabilization via Covalent Immobilization on Highly Activated Glyoxyl-Agarose
inferredcites →https://doi.org/10.1021/la4047512openalex-snapshot
Heterofunctional Hydrophilic–Hydrophobic Porous Silica as Support for Multipoint Covalent Immobilization of Lipases: Application to Lactulose Palmitate Synthesis
inferredcites →https://doi.org/10.1021/op0200165openalex-snapshot
Lipases from Candida antarctica: Unique Biocatalysts from a Unique Origin
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1038/351491a0openalex-snapshot
A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
inferredcites →https://doi.org/10.1038/362814a0openalex-snapshot
Interfacial activation of the lipase–procolipase complex by mixed micelles revealed by X-ray crystallography
inferredcites →https://doi.org/10.1039/c2cs35231aopenalex-snapshot
Modifying enzyme activity and selectivity by immobilization
inferredcites →https://doi.org/10.1039/c3cs35446fopenalex-snapshot
Immobilisation and application of lipases in organic media
inferredcites →https://doi.org/10.1039/c3cs60075kopenalex-snapshot
Enzyme immobilisation in biocatalysis: why, what and how
inferredcites →https://doi.org/10.1074/jbc.m808268200openalex-snapshot
Activation of Bacterial Thermoalkalophilic Lipases Is Spurred by Dramatic Structural Rearrangements
inferredcites →https://doi.org/10.1128/aem.70.2.1249-1251.2004openalex-snapshot
Stabilization of Penicillin G Acylase from Escherichia coli : Site-Directed Mutagenesis of the Protein Surface To Increase Multipoint Covalent Attachment
inferredcites →https://doi.org/10.3390/molecules19078995openalex-snapshot
Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4645398openalex-extracted
Immobilization of Candida Antarctic Lipase B by Macroporous Resin Adsorption and Organic Polymer Coating: Preparation, Characterization, and its Application for Biodiesel Production
inferred← citeshttps://doi.org/10.1002/bab.2098openalex-snapshot
An overview on the conversion of glycerol to value‐added industrial products via chemical and biochemical routes
inferred← citeshttps://doi.org/10.1002/bbb.2517openalex-snapshot
Production of sugars from mixed hardwoods for use in the synthesis of sugar fatty acid esters catalyzed by immobilized‐stabilized derivatives of Candida antarctica lipase B
inferred← citeshttps://doi.org/10.1002/btpr.2630openalex-snapshot
Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350
inferred← citeshttps://doi.org/10.1002/btpr.2735openalex-snapshot
Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica
inferred← citeshttps://doi.org/10.1002/cctc.201500310openalex-snapshot
Importance of the Support Properties for Immobilization or Purification of Enzymes
inferred← citeshttps://doi.org/10.1002/cctc.201901464openalex-snapshot
Immobilization of γ‐Glutamyl Transpeptidase from Equine Kidney for the Synthesis of kokumi Compounds
inferred← citeshttps://doi.org/10.1002/slct.201600274openalex-snapshot
Advantages of Heterofunctional Octyl Supports: Production of 1,2‐Dibutyrin by Specific and Selective Hydrolysis of Tributyrin Catalyzed by Immobilized Lipases
inferred← citeshttps://doi.org/10.1002/tcr.201600007openalex-snapshot
Chemical Modification in the Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities
inferred← citeshttps://doi.org/10.1007/978-3-030-10480-1_11openalex-snapshot
Fungal Lipases: Versatile Tools for White Biotechnology
inferred← citeshttps://doi.org/10.1007/978-981-33-6056-3_4openalex-snapshot
Chitosan Nanoparticle: Alternative for Sustainable Agriculture
inferred← citeshttps://doi.org/10.1007/s00449-019-02159-wopenalex-snapshot
Benzyl propionate synthesis by fed-batch esterification using commercial immobilized and lyophilized Cal B lipase
inferred← citeshttps://doi.org/10.1007/s00449-020-02411-8openalex-snapshot
Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate
inferred← citeshttps://doi.org/10.1007/s00449-024-03099-wopenalex-snapshot
Improved catalytic stability of immobilized Candida antarctica lipase B on macroporous resin with organic polymer coating for biodiesel production
inferred← citeshttps://doi.org/10.1007/s11947-026-04584-8openalex-snapshot
Immobilization of CALB on Semi-Janus Particles Improves Its Performance in Biphasic Synthesis of DHA Glycerides
inferred← citeshttps://doi.org/10.1007/s12010-022-03913-9openalex-snapshot
Activation and Stabilization of Lipase B from Candida antarctica by Immobilization on Polymer Brushes with Optimized Surface Structure
inferred← citeshttps://doi.org/10.1007/s43153-021-00218-yopenalex-snapshot
Applicability of mesoporous silica type SBA-15 as feasible support for the immobilization of Yarrowia lipolytica lipase and Candida antarctica lipase B
inferred← citeshttps://doi.org/10.1016/bs.mie.2015.09.035openalex-snapshot
Immobilization of Lipases on Heterofunctional Octyl–Glyoxyl Agarose Supports
inferred← citeshttps://doi.org/10.1016/j.bbapap.2019.06.005openalex-snapshot
Immobilization of lipase from Pseudomonas fluorescens on glyoxyl-octyl-agarose beads: Improved stability and reusability
inferred← citeshttps://doi.org/10.1016/j.bej.2018.07.003openalex-snapshot
Highly stable adsorptive and covalent immobilization of Thermomyces lanuginosus lipase on tailor-made porous carbon material
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2015.03.006openalex-snapshot
Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2018.06.002openalex-snapshot
Integrating enzyme immobilization and protein engineering: An alternative path for the development of novel and improved industrial biocatalysts
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2019.04.003openalex-snapshot
Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2020.107581openalex-snapshot
Lipase immobilization on ceramic supports: An overview on techniques and materials
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2020.107584openalex-snapshot
Enzyme co-immobilization: Always the biocatalyst designers' choice…or not?
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2021.107821openalex-snapshot
Stabilization of enzymes via immobilization: Multipoint covalent attachment and other stabilization strategies
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2023.108215openalex-snapshot
Biocatalytic production of biolubricants: Strategies, problems and future trends
inferred← citeshttps://doi.org/10.1016/j.btre.2017.02.003openalex-snapshot
Immobilization of CALB on activated chitosan: Application to enzymatic synthesis in supercritical and near-critical carbon dioxide
inferred← citeshttps://doi.org/10.1016/j.btre.2021.e00659openalex-snapshot
Ethanol as additive enhance the performance of immobilized lipase LipA from Pseudomonas aeruginosa on polypropylene support
inferred← citeshttps://doi.org/10.1016/j.cattod.2015.05.027openalex-snapshot
Chemical amination of lipases improves their immobilization on octyl-glyoxyl agarose beads
inferred← citeshttps://doi.org/10.1016/j.cattod.2020.03.059openalex-snapshot
Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2016.09.010openalex-snapshot
Relevance of substrates and products on the desorption of lipases physically adsorbed on hydrophobic supports
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2016.12.002openalex-snapshot
Effect of protein load on stability of immobilized enzymes
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2017.07.001openalex-snapshot
Improved stability of immobilized lipases via modification with polyethylenimine and glutaraldehyde
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2022.110166openalex-snapshot
Immobilization of Thermomyces lanuginosus lipase on a new hydrophobic support (Streamline phenyl™): Strategies to improve stability and reusability
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2025.110583openalex-snapshot
Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2026.110932openalex-snapshot
Evaluation of steam-exploded green coconut fiber as support for the immobilization of lipases from Pseudomonas fluorescens, Candida antarctica B, and Eversa
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A hydroesterification reaction system to produce octyl esters using degummed soybean oil as substrate: Combining reusable free and immobilized lipases
inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e32673openalex-snapshot
Current status and emerging frontiers in enzyme engineering: An industrial perspective
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Immobilization of lipases in hydrophobic chitosan for selective hydrolysis of fish oil: The impact of support functionalization on lipase activity, selectivity and stability
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2018.04.112openalex-snapshot
Use of chitosan heterofunctionality for enzyme immobilization: β-galactosidase immobilization for galacto-oligosaccharide synthesis
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New applications of glyoxyl-octyl agarose in lipases co-immobilization: Strategies to reuse the most stable lipase
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Further stabilization of lipase from Pseudomonas fluorescens immobilized on octyl coated nanoparticles via chemical modification with bifunctional agents
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Utilization of two modified layered doubled hydroxides as supports for immobilization of Candida rugosa lipase
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Optimization of immobilization conditions of Bacillus atrophaeus FSHM2 lipase on maleic copolymer coated amine-modified graphene oxide nanosheets and its application for valeric acid esterification
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Immobilized lipases-based nano-biocatalytic systems — A versatile platform with incredible biotechnological potential
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Chemical and physical Chitosan modification for designing enzymatic industrial biocatalysts: How to choose the best strategy?
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2021.09.061openalex-snapshot
Enzyme-support interactions and inactivation conditions determine Thermomyces lanuginosus lipase inactivation pathways: Functional and florescence studies
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.02.084openalex-snapshot
Coimmobilization of lipases exhibiting three very different stability ranges. Reuse of the active enzymes and selective discarding of the inactivated ones
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.03.151openalex-snapshot
Chemical amination of immobilized enzymes for enzyme coimmobilization: Reuse of the most stable immobilized and modified enzyme
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2024.133555openalex-snapshot
Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions
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A comprehensive review of lipase-catalyzed acidolysis as a method for producing structured glycerides
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2025.143305openalex-snapshot
Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2025.146777openalex-snapshot
Multiple co-interactions of different parameters on the functional properties of immobilized lipases
inferred← citeshttps://doi.org/10.1016/j.indcrop.2024.120014openalex-snapshot
Improving the performance of lipases in the full hydrolysis of residual coconut oil by immobilization on hydrophobic supports
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A novel and efficient method for punicic acid-enriched diacylglycerol preparation: Enzymatic ethanolysis of pomegranate seed oil catalyzed by Lipozyme 435
inferred← citeshttps://doi.org/10.1016/j.mcat.2019.110405openalex-snapshot
Lecitase ultra: A phospholipase with great potential in biocatalysis
inferred← citeshttps://doi.org/10.1016/j.mcat.2022.112540openalex-snapshot
Chemoenzymatic synthesis of both enantiomers of propafenone hydrochloride through lipase-catalyzed process
inferred← citeshttps://doi.org/10.1016/j.molcatb.2016.03.002openalex-snapshot
Reversible immobilization of lipases on octyl-glutamic agarose beads: A mixed adsorption that reinforces enzyme immobilization
inferred← citeshttps://doi.org/10.1016/j.molcatb.2016.05.007openalex-snapshot
Cashew apple bagasse as a support for the immobilization of lipase B from Candida antarctica: Application to the chemoenzymatic production of (R)-Indanol
inferred← citeshttps://doi.org/10.1016/j.molcatb.2016.08.008openalex-snapshot
Evaluation of different immobilized lipases in transesterification reactions using tributyrin: Advantages of the heterofunctional octyl agarose beads
inferred← citeshttps://doi.org/10.1016/j.procbio.2015.03.018openalex-snapshot
Evaluation of divinylsulfone activated agarose to immobilize lipases and to tune their catalytic properties
inferred← citeshttps://doi.org/10.1016/j.procbio.2015.05.010openalex-snapshot
Immobilization of lipases on glyoxyl–octyl supports: Improved stability and reactivation strategies
inferred← citeshttps://doi.org/10.1016/j.procbio.2015.06.023openalex-snapshot
Accurel MP 1000 as a support for the immobilization of lipase from Burkholderia cepacia : Application to the kinetic resolution of myo -inositol derivatives
inferred← citeshttps://doi.org/10.1016/j.procbio.2015.06.025openalex-snapshot
Selectivity of R-α-monobenzoate glycerol synthesis catalyzed by Candida antarctica lipase B immobilized on heterofunctional supports
inferred← citeshttps://doi.org/10.1016/j.procbio.2015.11.015openalex-snapshot
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2
inferred← citeshttps://doi.org/10.1016/j.procbio.2016.04.002openalex-snapshot
Easy stabilization of interfacially activated lipases using heterofunctional divinyl sulfone activated-octyl agarose beads. Modulation of the immobilized enzymes by altering their nanoenvironment
inferred← citeshttps://doi.org/10.1016/j.procbio.2016.09.016openalex-snapshot
Improved catalytic properties of Candida antarctica lipase B multi-attached on tailor-made hydrophobic silica containing octyl and multifunctional amino- glutaraldehyde spacer arms
inferred← citeshttps://doi.org/10.1016/j.procbio.2016.12.018openalex-snapshot
Physical crosslinking of lipase from Rhizomucor miehei immobilized on octyl agarose via coating with ionic polymers
inferred← citeshttps://doi.org/10.1016/j.procbio.2017.02.024openalex-snapshot
Effect of immobilization rate and enzyme crowding on enzyme stability under different conditions. The case of lipase from Thermomyces lanuginosus immobilized on octyl agarose beads
inferred← citeshttps://doi.org/10.1016/j.procbio.2017.02.025openalex-snapshot
Bleached kenaf microfiber as a support matrix for cyclodextrin glucanotransferase immobilization via covalent binding by different coupling agents
inferred← citeshttps://doi.org/10.1016/j.procbio.2017.06.014openalex-snapshot
Coimmobilization of enzymes in bilayers using pei as a glue to reuse the most stable enzyme: Preventing pei release during inactivated enzyme desorption
inferred← citeshttps://doi.org/10.1016/j.procbio.2017.07.018openalex-snapshot
Effect of high salt concentrations on the stability of immobilized lipases: Dramatic deleterious effects of phosphate anions
inferred← citeshttps://doi.org/10.1016/j.procbio.2017.09.011openalex-snapshot
Lipase immobilization on functionalized mesoporous TiO 2 : Specific adsorption, hyperactivation and application in cinnamyl acetate synthesis
inferred← citeshttps://doi.org/10.1016/j.procbio.2017.09.020openalex-snapshot
A new heterofunctional amino-vinyl sulfone support to immobilize enzymes: Application to the stabilization of β-galactosidase from A spergillus oryzae
inferred← citeshttps://doi.org/10.1016/j.procbio.2018.01.028openalex-snapshot
Different strategies to immobilize lipase from Geotrichum candidum : Kinetic and thermodynamic studies
inferred← citeshttps://doi.org/10.1016/j.procbio.2019.11.026openalex-snapshot
Parameters necessary to define an immobilized enzyme preparation
inferred← citeshttps://doi.org/10.1016/j.procbio.2019.11.037openalex-snapshot
Optimal spacer arm microenvironment for the immobilization of recombinant Protein A on heterofunctional amino-epoxy agarose supports
inferred← citeshttps://doi.org/10.1016/j.procbio.2020.01.013openalex-snapshot
Selective immobilization of Bacillus subtilis lipase A from cell culture supernatant: Improving catalytic performance and thermal resistance
inferred← citeshttps://doi.org/10.1016/j.procbio.2020.02.025openalex-snapshot
Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions
inferred← citeshttps://doi.org/10.1016/j.procbio.2023.08.003openalex-snapshot
The nature of the buffer alters the effects of the chemical modification on the stability of immobilized lipases
inferred← citeshttps://doi.org/10.1016/j.procbio.2026.07.016openalex-snapshot
Modulating the catalytic performance of immobilized lipase: Influence of blocking agents and solid-phase physicochemical modifications
inferred← citeshttps://doi.org/10.1016/j.reactfunctpolym.2020.104613openalex-snapshot
On the taught new tricks of enzymes immobilization: An all-inclusive overview
inferred← citeshttps://doi.org/10.1016/j.renene.2019.08.048openalex-snapshot
Conversion of bio-oil extracted from Chlorella vulgaris micro algae to biodiesel via modified superparamagnetic nano-biocatalyst
inferred← citeshttps://doi.org/10.1016/j.renene.2020.09.117openalex-snapshot
Tosylated cloisite as a new heterofunctional carrier for covalent immobilization of lipase and its utilization for production of biodiesel from waste frying oil
inferred← citeshttps://doi.org/10.1016/j.renene.2020.10.071openalex-snapshot
Liquid lipase preparations designed for industrial production of biodiesel. Is it really an optimal solution?
inferred← citeshttps://doi.org/10.1021/acs.macromol.7b02361openalex-snapshot
Protection of Opening Lids: Very High Catalytic Activity of Lipase Immobilized on Core–Shell Nanoparticles
inferred← citeshttps://doi.org/10.1021/acsami.1c09660openalex-snapshot
The Encounter of Biomolecules in Metal–Organic Framework Micro/Nano Reactors
inferred← citeshttps://doi.org/10.1021/acscatal.6b00942openalex-snapshot
Opening Lids: Modulation of Lipase Immobilization by Graphene Oxides
inferred← citeshttps://doi.org/10.1021/acsomega.3c10004openalex-snapshot
Intensification of Enzymatic Sorbityl Laurate Production in Dissolved and Neat Systems under Conventional and Microwave Heating
inferred← citeshttps://doi.org/10.1021/acssuschemeng.1c01065openalex-snapshot
Advantages of Supports Activated with Divinyl Sulfone in Enzyme Coimmobilization: Possibility of Multipoint Covalent Immobilization of the Most Stable Enzyme and Immobilization via Ion Exchange of the Least Stable Enzyme
inferred← citeshttps://doi.org/10.1039/c5an01588jopenalex-snapshot
A SERS protocol as a potential tool to access 6-mercaptopurine release accelerated by glutathione-S-transferase
inferred← citeshttps://doi.org/10.1039/c5ra05611jopenalex-snapshot
A mixed-function-grafted magnetic mesoporous hollow silica microsphere immobilized lipase strategy for ultrafast transesterification in a solvent-free system
inferred← citeshttps://doi.org/10.1039/c5ra07379kopenalex-snapshot
Reactivation of lipases by the unfolding and refolding of covalently immobilized biocatalysts
inferred← citeshttps://doi.org/10.1039/c6ra10906copenalex-snapshot
Development of simple protocols to solve the problems of enzyme coimmobilization. Application to coimmobilize a lipase and a β-galactosidase
inferred← citeshttps://doi.org/10.1039/c6ra13350aopenalex-snapshot
Design of a core–shell support to improve lipase features by immobilization
inferred← citeshttps://doi.org/10.1039/c6ra21730copenalex-snapshot
Evaluation of different commercial hydrophobic supports for the immobilization of lipases: tuning their stability, activity and specificity
inferred← citeshttps://doi.org/10.1039/c7ob01880kopenalex-snapshot
Immobilized enzymes: understanding enzyme – surface interactions at the molecular level
inferred← citeshttps://doi.org/10.1039/c7tb01639eopenalex-snapshot
Polyethylenimine: a very useful ionic polymer in the design of immobilized enzyme biocatalysts
inferred← citeshttps://doi.org/10.1039/c8nj02561dopenalex-snapshot
SERS based protocol using flow glass-hemostix for detection of neuron-specific enolase in blood plasma
inferred← citeshttps://doi.org/10.1039/c9cy00415gopenalex-snapshot
Novozym 435: the “perfect” lipase immobilized biocatalyst?
inferred← citeshttps://doi.org/10.1039/d0gc03229hopenalex-snapshot
Biocatalytic microgels (μ-Gel zymes ): synthesis, concepts, and emerging applications
inferred← citeshttps://doi.org/10.1039/d1cy00696gopenalex-snapshot
Solvent-free esterifications mediated by immobilized lipases: a review from thermodynamic and kinetic perspectives
inferred← citeshttps://doi.org/10.1039/d2cs00083kopenalex-snapshot
Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization
inferred← citeshttps://doi.org/10.1039/d3re00420aopenalex-snapshot
A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles
inferred← citeshttps://doi.org/10.1080/10242422.2016.1278212openalex-snapshot
Optimization of the coating of octyl-CALB with ionic polymers to improve stability and decrease enzyme leakage
inferred← citeshttps://doi.org/10.1080/10826068.2021.1920034openalex-snapshot
Optimization of an organic solvent-tolerant lipase production by Staphylococcus capitis SH6. Immobilization for biodiesel production and biodegradation of waste greases
inferred← citeshttps://doi.org/10.14393/ufu.di.2022.91openalex-snapshot
Avaliação de estratégias de imobilização e estabilização de β-galactosidase de Bacillus licheniformis
inferred← citeshttps://doi.org/10.21203/rs.3.rs-158248/v1openalex-snapshot
Enantioselective Resolution of (R, S)-DMPM by a Adsorption-Covalent Crosslinked Esterase PAE07 from Pseudochrobactrum Asaccharolyticum WZZ003
inferred← citeshttps://doi.org/10.21203/rs.3.rs-4922648/v1openalex-snapshot
Improved catalytic stability of immobilized Candida antarctic lipase B on macroporous resin with organic polymer coating for biodiesel production
inferred← citeshttps://doi.org/10.3389/fbioe.2020.00036openalex-snapshot
Effects of Enzyme Loading and Immobilization Conditions on the Catalytic Features of Lipase From Pseudomonas fluorescens Immobilized on Octyl-Agarose Beads
inferred← citeshttps://doi.org/10.3389/fbioe.2023.1229300openalex-snapshot
Nature-inspired Enzyme engineering and sustainable catalysis: biochemical clues from the world of plants and extremophiles
inferred← citeshttps://doi.org/10.3390/beverages8020021openalex-snapshot
Galacto-Oligosaccharide (GOS) Synthesis during Enzymatic Lactose-Free Milk Production: State of the Art and Emerging Opportunities
inferred← citeshttps://doi.org/10.3390/books978-3-03921-575-1openalex-snapshot
Recent Advances in Biocatalysis and Metabolic Engineering for Biomanufacturing
inferred← citeshttps://doi.org/10.3390/catal10060605openalex-snapshot
One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates
inferred← citeshttps://doi.org/10.3390/catal10060697openalex-snapshot
Recent Trends in Biomaterials for Immobilization of Lipases for Application in Non-Conventional Media
inferred← citeshttps://doi.org/10.3390/catal10070798openalex-snapshot
Enantioselective Transesterification of Allyl Alcohols with (E)-4-Arylbut-3-en-2-ol Motif by Immobilized Lecitase™ Ultra
inferred← citeshttps://doi.org/10.3390/catal10101207openalex-snapshot
Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones
inferred← citeshttps://doi.org/10.3390/catal11091067openalex-snapshot
Stabilization of Lecitase Ultra® by Immobilization and Fixation of Bimolecular Aggregates. Release of Omega-3 Fatty Acids by Enzymatic Hydrolysis of Krill Oil
inferred← citeshttps://doi.org/10.3390/catal12020242openalex-snapshot
Immobilization of Lipases on Modified Silica Clay for Bio-Diesel Production: The Effect of Surface Hydrophobicity on Performance
inferred← citeshttps://doi.org/10.3390/catal13010108openalex-snapshot
Heterofunctional Methacrylate Beads Bearing Octadecyl and Vinyl Sulfone Groups: Tricks to Obtain an Interfacially Activated Lipase from Thermomyces lanuginosus and Covalently Attached to the Support
inferred← citeshttps://doi.org/10.3390/catal14020105openalex-snapshot
The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading
inferred← citeshttps://doi.org/10.3390/catal15040375openalex-snapshot
Immobilized Lipases in the Synthesis of Short-Chain Esters: An Overview of Constraints and Perspectives
inferred← citeshttps://doi.org/10.3390/catal8110511openalex-snapshot
Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features
inferred← citeshttps://doi.org/10.3390/catal9050487openalex-snapshot
Reuse of Lipase from Pseudomonas fluorescens via Its Step-by-Step Coimmobilization on Glyoxyl-Octyl Agarose Beads with Least Stable Lipases
inferred← citeshttps://doi.org/10.3390/catal9070622openalex-snapshot
Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System
inferred← citeshttps://doi.org/10.3390/catal9121035openalex-snapshot
Genipin as An Emergent Tool in the Design of Biocatalysts: Mechanism of Reaction and Applications
inferred← citeshttps://doi.org/10.3390/ijms19020553openalex-snapshot
Stabilization of Immobilized Lipases by Intense Intramolecular Cross-Linking of Their Surfaces by Using Aldehyde-Dextran Polymers
inferred← citeshttps://doi.org/10.3390/ijms20225807openalex-snapshot
Ethyl Butyrate Synthesis Catalyzed by Lipases A and B from Candida antarctica Immobilized onto Magnetic Nanoparticles. Improvement of Biocatalysts’ Performance under Ultrasonic Irradiation
inferred← citeshttps://doi.org/10.3390/ijms21186501openalex-snapshot
Chemoenzymatic Synthesis of the New 3-((2,3-Diacetoxypropanoyl)oxy)propane-1,2-diyl Diacetate Using Immobilized Lipase B from Candida antarctica and Pyridinium Chlorochromate as an Oxidizing Agent
inferred← citeshttps://doi.org/10.3390/ijms23179933openalex-snapshot
Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks
inferred← citeshttps://doi.org/10.3390/ijms232214268openalex-snapshot
Immobilization of Lipase B from Candida antarctica in Octyl-Vinyl Sulfone Agarose: Effect of the Enzyme-Support Interactions on Enzyme Activity, Specificity, Structure and Inactivation Pathway
inferred← citeshttps://doi.org/10.3390/molecules21050646openalex-snapshot
Reversible Immobilization of Lipases on Heterofunctional Octyl-Amino Agarose Beads Prevents Enzyme Desorption
inferred← citeshttps://doi.org/10.3390/molecules21060751openalex-snapshot
Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI)
inferred← citeshttps://doi.org/10.3390/molecules21111577openalex-snapshot
Agarose and Its Derivatives as Supports for Enzyme Immobilization
inferred← citeshttps://doi.org/10.3390/molecules22010091openalex-snapshot
Desorption of Lipases Immobilized on Octyl-Agarose Beads and Coated with Ionic Polymers after Thermal Inactivation. Stronger Adsorption of Polymers/Unfolded Protein Composites
inferred← citeshttps://doi.org/10.3390/molecules22020212openalex-snapshot
Immobilized Lipases on Functionalized Silica Particles as Potential Biocatalysts for the Synthesis of Fructose Oleate in an Organic Solvent/Water System
inferred← citeshttps://doi.org/10.3390/molecules23020501openalex-snapshot
Kinetics and Optimization of Lipophilic Kojic Acid Derivative Synthesis in Polar Aprotic Solvent Using Lipozyme RMIM and Its Rheological Study
inferred← citeshttps://doi.org/10.3390/molecules23040766openalex-snapshot
Performance of Different Immobilized Lipases in the Syntheses of Short- and Long-Chain Carboxylic Acid Esters by Esterification Reactions in Organic Media
inferred← citeshttps://doi.org/10.3390/molecules23113015openalex-snapshot
Production of Omegas-6 and 9 from the Hydrolysis of Açaí and Buriti Oils by Lipase Immobilized on a Hydrophobic Support
inferred← citeshttps://doi.org/10.3390/molecules24183227openalex-snapshot
Synthesis with Immobilized Lipases and Downstream Processing of Ascorbyl Palmitate
inferred← citeshttps://doi.org/10.3390/molecules25051067openalex-snapshot
Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters
inferred← citeshttps://doi.org/10.3390/molecules26061574openalex-snapshot
Modulation of the Biocatalytic Properties of a Novel Lipase from Psychrophilic Serratia sp. (USBA-GBX-513) by Different Immobilization Strategies
inferred← citeshttps://doi.org/10.3390/molecules26113317openalex-snapshot
Lipozyme 435-Mediated Synthesis of Xylose Oleate in Methyl Ethyl Ketone
inferred← citeshttps://doi.org/10.3390/molecules29071467openalex-snapshot
Various Strategies for the Immobilization of a Phospholipase C from Bacillus cereus for the Modulation of Its Biochemical Properties
inferred← citeshttps://doi.org/10.3390/molecules30040939openalex-snapshot
A Comprehensive Guide to Enzyme Immobilization: All You Need to Know
inferred← citeshttps://doi.org/10.3390/molecules31040691openalex-snapshot
Poly (Ethylene-Alt-Maleic Anhydride) Ionic Modification of Lipase B from Candida antarctica Immobilized on Octyl Agarose Beads Alters Its Catalytic Properties
inferred← citeshttps://doi.org/10.3390/polym12091907openalex-snapshot
Enzymatic Polycondensation of 1,6-Hexanediol and Diethyl Adipate: A Statistical Approach Predicting the Key-Parameters in Solution and in Bulk
inferred← citeshttps://doi.org/10.5151/cobeq2018-pt.0855openalex-snapshot
PERFORMANCE DA IMOBILIZAÇÃO DE CALB EM QUITOSANA-VINILSULFONA E SUA APLICAÇÃO NA HIDRÓLISE DE (R,S) MANDELATO DE METILA
inferred← citeshttps://doi.org/10.70675/429ea2efz9059z40e8zb4dez4d2601219512openalex-snapshot
Enzymatic synthesis of DHA-lysophosphatidylcholine and evaluation of its effect on the MDA-MB-231 human breast cancer cell line
inferred← citeshttps://doi.org/10.70675/b1ef1a77z5ed6z4214zbd5bz81d8c68df07fopenalex-snapshot
Enzyme-catalyzed synthesis of polyesters by step-growth polymerization : a promising approach towards a greener synthetic pathway
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