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José C. S. dos Santos

Bio: 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.

Papers published on a yearly basis

Papers
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Journal ArticleDOI
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.
Abstract: We gratefully recognize the support from the Spanish Government, CTQ2013-41507-R, Colciencia (Colombia) and CNPq (Brazil). The predoctoral fellowships for Mr dos Santos (CNPq, Brazil) are also recognized. A. Berenguer-Murcia thanks the Spanish Ministerio de Ciencia e Innovaciun for a Ramon y Cajal fellowship (RyC-2009-03813).

465 citations

Journal ArticleDOI
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.

410 citations

Journal ArticleDOI
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.

364 citations

Journal ArticleDOI
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.
Abstract: This review discusses the possible roles of polyethylenimine (PEI) in the design of improved immobilized biocatalysts from diverse perspectives. This includes their use to activate supports and immobilize enzymes via ion exchange, as well as to improve immobilized enzymes by coating with PEI. PEI is a polymer containing primary, secondary and tertiary amino groups, having a strong anion exchange capacity under a broad range of conditions, and the capability to chemically react with different moieties on either an enzyme or a support. Also, as a multifunctional polymer, it has been modified stepwise to introduce different functionalities into the same polymer. This polymer (in combination with other anionic ones) permits the generation of “saline” environments around enzyme molecules, improving enzyme stability in the presence of hydrophobic compounds. The use of PEI as a physical glue useful to crosslink enzyme subunits in multimeric enzymes, monomeric enzymes immobilized via physical interactions or production of enzyme multilayers will be specially emphasized as new open avenues for enzyme coimmobilization. The coimmobilization of enzymes and cofactors using PEI may become one of the future developments allowed through an adequate use of this polymer and new pathways towards the design of enzyme combi-catalysts for their use in cascade reactions. Some unexplored but suggested uses derived from the properties of PEI are also proposed in the review, like the use of the buffering power of this multifunctional polymer to avoid pH gradients inside biocatalyst particles. Thus, 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.

208 citations


Cited by
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Journal Article
TL;DR: A method using scanning electron microscope to study the morphology of the bacterial and fungal microbes and thus determining antimicrobial activity is presented in the chapter.
Abstract: This study was conducted to identify and evaluate the antimicrobial activity of some Lactobacillus isolates of chicken origin. Among 90 isolates 14 Lactobacillus species were distinguished using MALDI-TOF mass spectrometry and 16S-ARDRA. The dominant species was L. salivarius (34.4%), followed by L. johnsonii (23.3%), L. crispatus (13.3%) and L. reuteri (11.1%). All lactobacilli were screened for antimicrobial activity against wild-type strains of Salmonella enterica, Escherichia coli, and Clostridium perfringens. Results from the agar slab method showed that all Lactobacillus isolates were able to produce active compounds on solid media with antagonistic properties against these pathogens. The highest sensitivity to lactobacilli was observed in C. perfringens strains, and the lowest in E. coli. Lactobacillus salivarius exhibited particularly strong antagonism towards all of the indicator bacteria. Strains of L. ingluviei and L. johnsonii and one strain of L. salivarius (10d) selectively inhibited the growth of C. perfringens. No antimicrobial activity of many Lactobacillus isolates was observed when cell-free culture supernatant was used in a well diffusion assay. All Lactobacillus isolates exhibited the ability to produce H2O2 and proved to be hydrophobic (excluding one of L. salivarius). [Int Microbiol 19(1):57-67 (2016)]Keywords: Lactobacillus spp. · avian lactobacilli · antimicrobial activity · gut health · poultry pathogens

767 citations

Journal ArticleDOI
TL;DR: The development of tailor-made heterofunctional supports as a tool to immobilize-stabilize-purify some proteins will be discussed in deep, using low concentration of adsorbent groups and a dense layer of groups able to give an intense multipoint covalent attachment.

545 citations

Journal ArticleDOI
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.
Abstract: We gratefully recognize the support from the Spanish Government, CTQ2013-41507-R, Colciencia (Colombia) and CNPq (Brazil). The predoctoral fellowships for Mr dos Santos (CNPq, Brazil) are also recognized. A. Berenguer-Murcia thanks the Spanish Ministerio de Ciencia e Innovaciun for a Ramon y Cajal fellowship (RyC-2009-03813).

465 citations

Journal ArticleDOI
TL;DR: A series of large-scale applications of immobilized enzymes with benefits for the food, chemical, pharmaceutical, cosmetics and medical device industries, some of which have been scarcely reported on previously are presented.

427 citations