J
Jose M. Palomo
Researcher at Spanish National Research Council
Publications - 165
Citations - 10743
Jose M. Palomo is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Lipase & Candida antarctica. The author has an hindex of 47, co-authored 153 publications receiving 9774 citations. Previous affiliations of Jose M. Palomo include Autonomous University of Madrid & Max Planck Society.
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Journal ArticleDOI
Improvement of enzyme activity, stability and selectivity via immobilization techniques
Cesar Mateo,Jose M. Palomo,Gloria Fernández-Lorente,Jose M. Guisan,Roberto Fernandez-Lafuente +4 more
TL;DR: In all cases, enzyme engineering via immobilization techniques is perfectly compatible with other chemical or biological approaches to improve enzyme functions and the final success depend on the availability of a wide battery of immobilization protocols.
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Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases
Jose M. Palomo,Gloria Muñoz,Gloria Fernández-Lorente,Cesar Mateo,Roberto Fernandez-Lafuente,Jose M. Guisan +5 more
TL;DR: It seems that the “open structure” of lipases, adsorbed on hydrophobic supports, is much more active and much more stable than the corresponding “closed” structure even when the closed structure is undergoing a very intense multipoint covalent attachment.
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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.
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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.
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A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates.
TL;DR: It is proposed that macromolecular cross‐linkers are too large to penetrate the protein active site and react with catalytically essential amino acid residues.