0000000000423656

AUTHOR

María Mormeneo

showing 3 related works from this author

Differential behaviour of Pseudomonas sp. 42A2 LipC, a lipase showing greater versatility than its counterpart LipA

2009

Abstract Growth of Pseudomonas sp. 42A2 on oleic acid releases polymerized hydroxy-fatty acids as a result of several enzymatic conversions that could involve one or more lipases. To test this hypothesis, the lipolytic system of strain Pseudomonas sp. 42A2 was analyzed, revealing the presence of at least an intracellular carboxylesterase and a secreted lipase. Consensus primers derived from a conserved region of bacterial lipase subfamilies I.1 and I.2 allowed isolation of two secreted lipase genes, lipA and lipC, highly homologous to those of Pseudomonas aeruginosa PAO1. Homologous cloning of the isolated lipA and lipC genes was performed in Pseudomonas sp. 42A2 for LipA and LipC over-expr…

chemistry.chemical_classificationbiologyStrain (chemistry)PseudomonasFatty acidLipaseGeneral Medicinebiology.organism_classificationBiochemistrySubstrate SpecificityIsoenzymesCarboxylesteraseOleic acidchemistry.chemical_compoundEnzymeBacterial ProteinschemistryBiochemistryPseudomonasEnzyme Stabilitybiology.proteinEnzyme kineticsLipaseBiochimie
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Translational fusion to the Pir4 cell wall protein as a general and efficient method for cell surface immobilization or growth medium secretion of re…

2008

chemistry.chemical_classificationGrowth mediumbiologyChemistrySaccharomyces cerevisiaeCellBioengineeringGeneral Medicinebiology.organism_classificationApplied Microbiology and Biotechnologylaw.inventionCell wallchemistry.chemical_compoundEnzymemedicine.anatomical_structureBiochemistryAntigenlawmedicineRecombinant DNASecretionBiotechnologyJournal of Biotechnology
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Efficient expression of a Paenibacillus barcinonensis endoglucanase in Saccharomyces cerevisiae.

2011

Abstract The endoglucanase coded by celA (GenBank Access No. Y12512) from Paenibacillus barcinonensis, an enzyme with good characteristics for application on paper manufacture from agricultural fibers, was expressed in Saccharomyces cerevisiae by using different domains of the cell wall protein Pir4 as translational fusion partners, to achieve either secretion or cell wall retention of the recombinant enzyme. Given the presence of five potential N-glycosylation sites in the amino acid sequence coded by celA, the effect of glycosylation on the enzymatic activity of the recombinant enzyme was investigated by expressing the recombinant fusion proteins in both, standard and glycosylation-defici…

GlycosylationGlycosylationSaccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeBioengineeringCellulaseSaccharomyces cerevisiaeApplied Microbiology and Biotechnologylaw.inventionchemistry.chemical_compoundBacterial ProteinsCellulaselawPeptide sequencechemistry.chemical_classificationbiologybiology.organism_classificationFusion proteinYeastEnzymeBiochemistrychemistryBatch Cell Culture TechniquesRecombinant DNAbiology.proteinPaenibacillusBiotechnologyJournal of industrial microbiologybiotechnology
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