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Oveimar Barbosa

Researcher at Universidad del Tolima

Publications -  57
Citations -  5552

Oveimar Barbosa is an academic researcher from Universidad del Tolima. The author has contributed to research in topics: Immobilized enzyme & Candida antarctica. The author has an hindex of 35, co-authored 55 publications receiving 4305 citations. Previous affiliations of Oveimar Barbosa include Spanish National Research Council & Industrial University of Santander.

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Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization

TL;DR: Glutaraldehyde, an apparently old fashioned reactive, remains the most widely used and with broadest application possibilities among the compounds used for the design of biocatalyst.
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Strategies for the one-step immobilization–purification of enzymes as industrial biocatalysts

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.
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Importance of the Support Properties for Immobilization or Purification of Enzymes

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.
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Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties.

TL;DR: This Review will discuss the suitable properties of the groups able to give the covalent attachment, and the groups unable to produce the first enzyme adsorption on the support, as well as the likely pathways for the evolution.
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Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions.

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.