JAVIER
ROCHA MARTÍN
Profesor ayudante doctor
Consejo Superior de Investigaciones Científicas
Madrid, EspañaPublicacions en col·laboració amb investigadors/es de Consejo Superior de Investigaciones Científicas (40)
2024
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Adsorption features of reduced aminated supports modified with glutaraldehyde: Understanding the heterofunctional features of these supports
International Journal of Biological Macromolecules, Vol. 263
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Reutilization of the Most Stable Coimmobilized Enzyme Using Glutaraldehyde Chemistry to Produce a New Combi-biocatalyst When the Coimmobilized Enzyme with a Lower Stability Is Inactivated
ACS Sustainable Chemistry and Engineering, Vol. 12, Núm. 17, pp. 6564-6572
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The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading
Catalysts, Vol. 14, Núm. 2
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The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support
Biotechnology Progress, Vol. 40, Núm. 1
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Tuning Almond Lipase Features by Using Different Immobilization Supports
Catalysts, Vol. 14, Núm. 2
2023
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Biocatalytic production of biolubricants: Strategies, problems and future trends
Biotechnology Advances, Vol. 68
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Glutaraldehyde modification of lipases immobilized on octyl agarose beads: Roles of the support enzyme loading and chemical amination of the enzyme on the final enzyme features
International Journal of Biological Macromolecules, Vol. 248
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Glyoxyl-ficin: An example where a more intense multipoint covalent attachment may decrease enzyme stability.
Process Biochemistry, Vol. 132, pp. 289-296
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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
Catalysts, Vol. 13, Núm. 1
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Synergy of Ion Exchange and Covalent Reaction: Immobilization of Penicillin G Acylase on Heterofunctional Amino-Vinyl Sulfone Agarose
Catalysts, Vol. 13, Núm. 1
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The nature of the buffer alters the effects of the chemical modification on the stability of immobilized lipases
Process Biochemistry, Vol. 133, pp. 20-27
2022
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Chemical amination of immobilized enzymes for enzyme coimmobilization: Reuse of the most stable immobilized and modified enzyme
International Journal of Biological Macromolecules, Vol. 208, pp. 688-697
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Coimmobilization of lipases exhibiting three very different stability ranges. Reuse of the active enzymes and selective discarding of the inactivated ones
International Journal of Biological Macromolecules, Vol. 206, pp. 580-590
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Determination of immobilized lipase stability depends on the substrate and activity determination condition: Stress inactivations and optimal temperature as biocatalysts stability indicators
Sustainable Chemistry and Pharmacy, Vol. 29
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Enzyme immobilization strategies for the design of robust and efficient biocatalysts
Current Opinion in Green and Sustainable Chemistry, Vol. 35
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Immobilization of Penicillin G Acylase on Vinyl Sulfone-Agarose: An Unexpected Effect of the Ionic Strength on the Performance of the Immobilization Process
Molecules, Vol. 27, Núm. 21
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Immobilization-stabilization of the dimeric D-amino acid oxidase from porcine kidney
Process Biochemistry, Vol. 122, pp. 120-128
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Mineralization of Lipase from Thermomyces lanuginosus Immobilized on Methacrylate Beads Bearing Octadecyl Groups to Improve Enzyme Features
Catalysts, Vol. 12, Núm. 12
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Preparation of a Six-Enzyme Multilayer Combi-Biocatalyst: Reuse of the Most Stable Enzymes after Inactivation of the Least Stable One
ACS Sustainable Chemistry and Engineering, Vol. 10, Núm. 12, pp. 3920-3934
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Stabilization of immobilized lipases by treatment with metallic phosphate salts
International Journal of Biological Macromolecules, Vol. 213, pp. 43-54