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Daniel Hormigo

Researcher at Complutense University of Madrid

Publications -  16
Citations -  243

Daniel Hormigo is an academic researcher from Complutense University of Madrid. The author has contributed to research in topics: Confocal scanning microscopy & Actinoplanes utahensis. The author has an hindex of 9, co-authored 16 publications receiving 218 citations. Previous affiliations of Daniel Hormigo include European University of Madrid & Spanish National Research Council.

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Preparation and characterization of cross-linked enzyme aggregates (CLEAs) of recombinant poly-3-hydroxybutyrate depolymerase from Streptomyces exfoliatus.

TL;DR: Cross-linked enzyme aggregates of poly-3-hydroxybutyrate (PHB) depolymerase from Streptomyces exfoliatus (PhaZ(Sex)-CLEAs) showed higher pH and temperature stability, and better tolerance to several organic solvents than its soluble counterpart.
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Novel extracellular PHB depolymerase from Streptomyces ascomycinicus: PHB copolymers degradation in acidic conditions.

TL;DR: Structural results supported the proposal of a three-dimensional model for this PHB depolymerase, and the features shown by PhaZSa make it an interesting candidate for industrial applications involving PHB degradation.
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Newly Discovered Penicillin Acylase Activity of Aculeacin A Acylase from Actinoplanes utahensis

TL;DR: Aculeacin A acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins are revealed in Actinoplanes utahensis produced by Streptomyces lividans.
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Extracellular production of Streptomyces exfoliatus poly(3-hydroxybutyrate) depolymerase in Rhodococcus sp. T104: determination of optimal biocatalyst conditions

TL;DR: High-performance liquid chromatography–mass spectrometry analysis of PHB products of enzymatic hydrolysis showed monomers and dimers of 3-hydroxybutyric acid, demonstrating that PHB depolymerase is an exo-hydrolase.
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Immobilized aculeacin A acylase from Actinoplanes utahensis: characterization of a novel biocatalyst.

TL;DR: Substrate specificity of the derivative showed its ability to efficiently hydrolyze other natural aliphatic penicillins such as penicillsins K, F and dihydroF besides its own substrate aculeacin A, which could allow its exploitation in industrial preparation of beta-lactam antibiotics and echinocandins.