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Your search keyword '"Mata, Isabel de la"' showing total 6 results
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6 results on '"Mata, Isabel de la"'

1. Integration of migrant and refugee data in health information systems in Europe: advancing evidence, policy and practice

Author

Bozorgmehr, Kayvan, McKee, Martin, Azzopardi-Muscat, Natasha, Bartovic, Jozef, Campos-Matos, Ines, Gerganova, Tsvetelina-Ivanova, Hannigan, Ailish, Janković, Jelena, Kállayová, Daniela, Kaplan, Josiah, Kayi, Ilker, Kondilis, Elias, Lundberg, Lene, Mata, Isabel de la, Medarević, Aleksandar, Suvada, Jozef, Wickramage, Kolitha, and Puthoopparambil, Soorej Jose

Published
2023
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4. Lactobacillus reuteri 2'-deoxyribosyltransferase, a novel biocatalyst for tailoring of nucleosides

Author

Fernandez-Lucas, Jesus, Acebal, Carmen, Sinisterra, Jose V., Arroyo, Miguel, and Mata, Isabel de la

Subjects
Deoxyribonucleotides -- Chemical properties, Gene expression -- Analysis, Lactobacillus -- Physiological aspects, Lactobacillus -- Genetic aspects, Biological sciences
Abstract

The cloning and expression of a putative ndt gene encoding a putative nucleoside 2'-deoxyribosyltransferase from Lactobacillus reuteri (LrNDT) is described. The findings from the study could be used to obtain a biocatalyst that could be used in industrial natural and nonnatural tailored nucleoside synthesis such as arabino- and 2'-fluoro-2'-deoxyribonucleoside analogues applied as potential therapeutic agents.

Published
2010

5. Novel extracellular medium-chain-length polyhydroxyalkanoate depolymerase from streptomyces exfoliatus DSMZ 41693: a promising biocatalyst for the efficient degradation of natural and functionalized mcl-PHAs

Author

Martínez, Virginia, Gómez de Santos, Patricia, García Hidalgo, Javier, Hormigo Cisneros, Daniel, Prieto, María Auxiliadora, Arroyo, Miguel, and Mata, Isabel de la

Subjects
Biotecnología, 3-Hydroxyalkanoic acids, Polyhydroxyalkanoate depolymerase, Streptomyces exfoliatus
Abstract

Cloning and biochemical characterization of a novel extracellular medium-chain-length polyhydroxyalkanoate (mcl-PHA) depolymerase from Streptomyces exfoliatus K10 DSMZ 41693 are described. The primary structure of the depolymerase (PhaZSex2) includes the lipase consensus sequence (serine-histidine-aspartic acid) which is known for serine hydrolases. Secondary structure analysis shows 7.9 % α-helix, 43.9 % β-sheet, 19.4 % β-turns, and 31.2 % random coil, suggesting that this enzyme belongs to the α/β hydrolase fold family, in agreement with other PHA depolymerases and lipases. The enzyme was efficiently produced as an extracellular active form in Rhodococcus and purified by two consecutive hydrophobic chromatographic steps. Matrix-assisted laser desorption-time-of-flight (MALDI-TOF) analysis of the purified enzyme revealed a monomer of 27.6 kDa with a midpoint transition temperature of 44.2 °C. Remarkably, the activity is significantly enhanced by low concentrations of nonionic and anionic detergents and thermal stability is improved by the presence of 10 % glycerol. 3.376 JCR (2015) Q2, 41/161 Biotechnology & applied microbiology UEM

Published
2015

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