Gloria Fernández-Lorente mainly focuses on Organic chemistry, Lipase, Hydrolysis, Enzyme and Immobilized enzyme. Her study in Covalent bond, Epoxy and Catalysis falls within the category of Organic chemistry. Her Lipase research integrates issues from Adsorption and Active site.
The study incorporates disciplines such as Enantiomer and Substrate in addition to Hydrolysis. Her Enzyme study incorporates themes from Molecule and Stereochemistry. Gloria Fernández-Lorente has researched Immobilized enzyme in several fields, including Combinatorial chemistry, Selectivity, Phenylacetic acid and Glutaraldehyde.
The scientist’s investigation covers issues in Organic chemistry, Lipase, Enzyme, Hydrolysis and Immobilized enzyme. Her Lipase research is multidisciplinary, incorporating elements of Glutaraldehyde and Chromatography. Her Enzyme research incorporates elements of Covalent bond, Molecule and Stereochemistry.
Her Covalent bond research includes elements of Amino acid, Aldehyde, Epoxy, Combinatorial chemistry and Nucleophile. Her Hydrolysis study integrates concerns from other disciplines, such as Enzyme assay, Regioselectivity, Substrate, Agarose and Enantiomer. Her study on Immobilized enzyme also encompasses disciplines like
Gloria Fernández-Lorente mostly deals with Enzyme, Immobilized enzyme, Organic chemistry, Catalysis and Lipase. Her Enzyme study incorporates themes from Covalent bond, Molecule, Stereochemistry and Lysine. Her Immobilized enzyme research incorporates themes from Catalase and Aldehyde.
All of her Organic chemistry and Hydrolysis and Hexane investigations are sub-components of the entire Organic chemistry study. Her Catalysis research integrates issues from Nanotechnology, Chemical process and Protein chemistry. Gloria Fernández-Lorente interconnects Acetone, Esterase, Enzyme kinetics and Adsorption in the investigation of issues within Lipase.
Gloria Fernández-Lorente mainly investigates Immobilized enzyme, Enzyme, Organic chemistry, Sunflower oil and Hexane. Her Immobilized enzyme research includes themes of Nuclear chemistry, Diamine oxidase, Catalysis, Aldehyde and Hydrogen peroxide. Her biological study spans a wide range of topics, including Covalent bond, Pisum and Agarose.
Covalent bond is frequently linked to Biochemistry in her study. Her work carried out in the field of Agarose brings together such families of science as Combinatorial chemistry, Hydrolysis and Xylan. Her studies deal with areas such as Adsorption, Mesoporous material, Ethyl oleate, Anhydrous and Lipase as well as Hexane.
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Improvement of enzyme activity, stability and selectivity via immobilization techniques
Cesar Mateo;Jose M. Palomo;Gloria Fernandez-Lorente;Jose M. Guisan.
Enzyme and Microbial Technology (2007)
Immobilization of lipases by selective adsorption on hydrophobic supports.
Roberto Fernandez-Lafuente;Pilar Armisén;Pilar Sabuquillo;Gloria Fernández-Lorente.
Chemistry and Physics of Lipids (1998)
Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases
José M Palomo;Gloria Muñoz;Gloria Fernández-Lorente;Cesar Mateo.
Journal of Molecular Catalysis B-enzymatic (2002)
Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins
César Mateo;José M. Palomo;Manuel Fuentes;Lorena Betancor.
Enzyme and Microbial Technology (2006)
Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage.
Cesar Mateo;Gloria Fernández-Lorente;Olga Abian;Roberto Fernández-Lafuente.
Epoxy sepabeads: a novel epoxy support for stabilization of industrial enzymes via very intense multipoint covalent attachment.
Cesar Mateo;Olga Abian;Gloria Fernandez-Lorente;Justo Pedroche.
Biotechnology Progress (2002)
Some special features of glyoxyl supports to immobilize proteins
Cesar Mateo;Olga Abian;Marieta Bernedo;Emma Cuenca.
Enzyme and Microbial Technology (2005)
Epoxy-Amino Groups: A New Tool for Improved Immobilization of Proteins by the Epoxy Method
Cesar Mateo;Rodrigo Torres;Gloria Fernández-Lorente;Claudia Ortiz.
General trend of lipase to self-assemble giving bimolecular aggregates greatly modifies the enzyme functionality.
Jose M. Palomo;Manuel Fuentes;Gloria Fernandez-Lorente;Cesar Mateo.
Modulation of the enantioselectivity of lipases via controlled immobilization and medium engineering: hydrolytic resolution of mandelic acid esters
Jose M Palomo;Gloria Fernandez-Lorente;Cesar Mateo;Claudia Ortiz.
Enzyme and Microbial Technology (2002)
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