J
José C. S. dos Santos
Researcher at University for International Integration of the Afro-Brazilian Lusophony
Publications - 85
Citations - 6230
José C. S. dos Santos is an academic researcher from University for International Integration of the Afro-Brazilian Lusophony. The author has contributed to research in topics: Immobilized enzyme & Lipase. The author has an hindex of 40, co-authored 74 publications receiving 3992 citations. Previous affiliations of José C. S. dos Santos include Spanish National Research Council & Federal University of Ceará.
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Journal ArticleDOI
Importance of the Support Properties for Immobilization or Purification of Enzymes
José C. S. dos Santos,José C. S. dos Santos,Oveimar Barbosa,Claudia Ortiz,Ángel Berenguer-Murcia,Rafael C. Rodrigues,Roberto Fernandez-Lafuente +6 more
TL;DR: This review will focus its attention on the requirements of a support surface to produce the desired objectives, the ideal physical properties of the matrix, the properties ofThe introduced reactive groups, the best surface activation degree to reach the desired objective, and the Properties of the reactive groups will be discussed.
Journal ArticleDOI
Immobilization of lipases on hydrophobic supports involves the open form of the enzyme
Evelin A. Manoel,Evelin A. Manoel,José C. S. dos Santos,José C. S. dos Santos,Denise M. G. Freire,Nazzoly Rueda,Roberto Fernandez-Lafuente +6 more
TL;DR: The results confirm that the lipases immobilized on octyl agarose presented their open form stabilized while the covalent preparation maintains a closing/opening equilibrium that may be modulated by altering the medium.
Journal ArticleDOI
Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions.
Rafael C. Rodrigues,Jose J. Virgen-Ortíz,José C. S. dos Santos,Ángel Berenguer-Murcia,Andrés R. Alcántara,Oveimar Barbosa,Claudia Ortiz,Roberto Fernandez-Lafuente +7 more
TL;DR: These immobilized lipases may be subject to unfolding and refolding strategies to reactivate inactivated enzymes, and these biocatalysts have been used in new strategies for enzyme coimmobilization, where the most stable enzyme could be reutilized after desorption of the least stable one after its inactivation.
Journal ArticleDOI
Novozym 435: the “perfect” lipase immobilized biocatalyst?
Claudia Ortiz,María Luján Ferreira,Oveimar Barbosa,José C. S. dos Santos,Rafael C. Rodrigues,Ángel Berenguer-Murcia,Laura E. Briand,Roberto Fernandez-Lafuente +7 more
TL;DR: Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes with its advantages and drawbacks.
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Polyethylenimine: a very useful ionic polymer in the design of immobilized enzyme biocatalysts.
Jose J. Virgen-Ortíz,José C. S. dos Santos,Ángel Berenguer-Murcia,Oveimar Barbosa,Rafael C. Rodrigues,Roberto Fernandez-Lafuente +5 more
TL;DR: Although PEI has been a largely popular polymer in biocatalyst design, it looks like a long and in some cases almost unexplored road lies ahead.