M
Manuel Fuentes
Researcher at Spanish National Research Council
Publications - 164
Citations - 5726
Manuel Fuentes is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Protein microarray & Immobilized enzyme. The author has an hindex of 38, co-authored 151 publications receiving 5113 citations. Previous affiliations of Manuel Fuentes include Valparaiso University & University of Genoa.
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Journal ArticleDOI
Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins
Cesar Mateo,Jose M. Palomo,Manuel Fuentes,Lorena Betancor,Valeria Grazú,Fernando López-Gallego,Benevides C. C. Pessela,Aurelio Hidalgo,Gloria Fernández-Lorente,Roberto Fernandez-Lafuente,Jose M. Guisan +10 more
TL;DR: Very active and highly stabilized derivatives of many enzymes and proteins have been prepared using activated supports that immobilize proteins, via a two-point reaction involving the region/s of the protein surface with the higher densities of amino groups.
Journal ArticleDOI
Next-generation high-density self-assembling functional protein arrays
Niroshan Ramachandran,Jacob Raphael,Eugenie Hainsworth,Gokhan Demirkan,Manuel Fuentes,Andreas Rolfs,Yanhui Hu,Joshua LaBaer +7 more
TL;DR: A high-density self-assembling protein microarray, based on the nucleic acid programmable protein array (NAPPA) concept, to display thousands of proteins that are produced and captured in situ from immobilized cDNA templates is developed.
Journal ArticleDOI
Some special features of glyoxyl supports to immobilize proteins
Cesar Mateo,Olga Abian,Marieta Bernedo,Emma Cuenca,Manuel Fuentes,Gloria Fernández-Lorente,Jose M. Palomo,Valeria Grazú,Benevides C. C. Pessela,Cecilia Giacomini,Cecilia Giacomini,Gabriela Irazoqui,Gabriela Irazoqui,Andrea Villarino,Andrea Villarino,Karen Ovsejevi,Karen Ovsejevi,Francisco Batista-Viera,Roberto Fernandez-Lafuente,Jose M. Guisan +19 more
TL;DR: This mechanism promotes that proteins become immobilized by the area/s where the highest lysine residues density is located and explain the high enzyme stabilization usually achieved by using this immobilization technique.
Journal ArticleDOI
Epoxy-Amino Groups: A New Tool for Improved Immobilization of Proteins by the Epoxy Method
Cesar Mateo,Rodrigo Torres,Gloria Fernández-Lorente,Claudia Ortiz,Manuel Fuentes,Aurelio Hidalgo,Fernando López-Gallego,Olga Abian,Jose M. Palomo,Lorena Betancor,Benevides C. C. Pessela,Jose M. Guisan,Roberto Fernandez-Lafuente +12 more
TL;DR: Stability of the immobilized enzyme has been found to be much higher using the new support than in preparations using the conventional ones in many cases, and immobilization is much more rapid using amino-epoxy supports than employing conventional epoxy supports.
Journal ArticleDOI
General trend of lipase to self-assemble giving bimolecular aggregates greatly modifies the enzyme functionality.
Jose M. Palomo,Manuel Fuentes,Gloria Fernández-Lorente,Cesar Mateo,Jose M. Guisan,Roberto Fernandez-Lafuente +5 more
TL;DR: Three microbial lipases (those from Candida rugosa, Humicola lanuginosa, and Mucor miehei) have been found to exhibit a tendency to form bimolecular aggregates in solution even at very low enzyme concentrations in the absence of a detergent.