Publicaciones en colaboración con investigadores/as de Consejo Superior de Investigaciones Científicas (46)

2024

  1. Adsorption features of reduced aminated supports modified with glutaraldehyde: Understanding the heterofunctional features of these supports

    International Journal of Biological Macromolecules, Vol. 263

  2. Changes in ficin specificity by different substrate proteins promoted by enzyme immobilization

    Enzyme and Microbial Technology, Vol. 181

  3. Designing mixed cationic/anionic supports to covalently immobilize/stabilize enzymes with high isoelectric point by enzyme adsorption and support-enzyme glutaraldehyde crosslinking

    International Journal of Biological Macromolecules, Vol. 280

  4. Designing tailor-made steric matters to improve the immobilized ficin specificity for small versus large proteins

    Journal of Biotechnology, Vol. 395, pp. 12-21

  5. 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

  6. Support Enzyme Loading Influences the Effect of Aldehyde Dextran Modification on the Specificity of Immobilized Ficin for Large Proteins

    Molecules, Vol. 29, Núm. 15

  7. Tailoring the specificity of ficin versus large hemoglobin and small casein by co-immobilizing inert proteins on the immobilized enzyme layer and further modification with aldehyde dextran

    International Journal of Biological Macromolecules, Vol. 277

  8. The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading

    Catalysts, Vol. 14, Núm. 2

  9. 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

  10. Tuning Almond Lipase Features by Using Different Immobilization Supports

    Catalysts, Vol. 14, Núm. 2

  11. Tuning almond lipase features by the buffer used during immobilization: The apparent biocatalysts stability depends on the immobilization and inactivation buffers and the substrate utilized

    Journal of Biotechnology, Vol. 391, pp. 72-80

2023

  1. Biocatalytic production of biolubricants: Strategies, problems and future trends

    Biotechnology Advances, Vol. 68

  2. 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

  3. Glyoxyl-ficin: An example where a more intense multipoint covalent attachment may decrease enzyme stability.

    Process Biochemistry, Vol. 132, pp. 289-296

  4. 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

  5. Synergy of Ion Exchange and Covalent Reaction: Immobilization of Penicillin G Acylase on Heterofunctional Amino-Vinyl Sulfone Agarose

    Catalysts, Vol. 13, Núm. 1

  6. 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

  1. 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

  2. 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

  3. 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