Search results for "Enzyme Stability"

showing 10 items of 37 documents

A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes

1999

The gene xynC encoding xylanase C from Bacillus sp. BP-23 was cloned and expressed in Escherichia coli. The nucleotide sequence of a 3538 bp DNA fragment containing xynC gene was determined, revealing an open reading frame of 3258 bp that encodes a protein of 120,567 Da. A comparison of the deduced amino acid sequence of xylanase C with known beta-glycanase sequences showed that the encoded enzyme is a modular protein containing three different domains. The central region of the enzyme is the catalytic domain, which shows high homology to family 10 xylanases. A domain homologous to family IX cellulose-binding domains is located in the C-terminal region of xylanase C, whilst the N-terminal r…

Molecular Sequence DataBacillusBiologymedicine.disease_causeMicrobiologyHomology (biology)Substrate Specificitychemistry.chemical_compoundCatalytic DomainEnzyme StabilityEscherichia colimedicineXylobioseAmino Acid SequenceCloning MolecularEscherichia coliPeptide sequencechemistry.chemical_classificationEndo-14-beta XylanasesSequence Homology Amino AcidThermophileTemperatureNucleic acid sequenceSequence Analysis DNAXylosidasesEnzymeBiochemistrychemistryGenes BacterialXylanaseSequence AlignmentMicrobiology
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C172S Substitution in the Chloroplast-encoded Large Subunit Affects Stability and Stress-induced Turnover of Ribulose-1,5-bisphosphate Carboxylase/Ox…

1999

Previous work has indicated that the turnover of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1. 39) may be controlled by the redox state of certain cysteine residues. To test this hypothesis, directed mutagenesis and chloroplast transformation were employed to create a C172S substitution in the Rubisco large subunit of the green alga Chlamydomonas reinhardtii. The C172S mutant strain was not substantially different from the wild type with respect to growth rate, and the purified mutant enzyme had a normal circular dichroism spectrum. However, the mutant enzyme was inactivated faster than the wild-type enzyme at 40 and 50 degrees C. In contrast, C172S mutant …

OxygenaseChloroplastsProtein ConformationRibulose-Bisphosphate CarboxylaseMutantChlamydomonas reinhardtiiBiochemistrychemistry.chemical_compoundEnzyme StabilitySerineAnimalsCysteineMolecular BiologyCysteine metabolismRibulose 15-bisphosphatebiologyCircular DichroismRuBisCOWild typeCell Biologybiology.organism_classificationChloroplastPhenotypeAmino Acid SubstitutionchemistryBiochemistryMutagenesis Site-Directedbiology.proteinSpectrophotometry UltravioletOxidation-ReductionChlamydomonas reinhardtiiJournal of Biological Chemistry
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Increased susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolytic degradation caused by oxidative treatments

1990

The susceptibility of the chloroplastic enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolysis by trypsin, chymotrypsin, proteinase K, and papain is enhanced by oxidative treatments including spontaneous oxidation of cysteines. Proteinases exhibit a high specificity for the oxidized inactive form of the carboxylase, cleaving its large subunit. Treatment of the inactive enzyme with dithiothreitol results in partial recovery of both carboxylase activity and resistance to proteolysis. This behavior may explain the specific degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase that occurs in vivo during leaf senescence.

OxygenaseTime FactorsRibulose-Bisphosphate CarboxylaseProteolysisBiophysicsBiochemistryDithiothreitolchemistry.chemical_compoundEnzyme StabilitymedicineCysteineMolecular Biologychemistry.chemical_classificationChymotrypsinRibulose 15-bisphosphatebiologymedicine.diagnostic_testHydrolysisPlantsTrypsinPyruvate carboxylaseEnzymechemistryBiochemistrybiology.proteinOxidation-ReductionPeptide Hydrolasesmedicine.drugArchives of Biochemistry and Biophysics
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Hydrolytic action of phospholipase A2 in monolayers in the phase transition region: direct observation of enzyme domain formation using fluorescence …

1990

Phospholipase A2, a ubiquitous lipolytic enzyme highly active in the hydrolysis of organized phospholipid substrates, has been characterized optically in its action against a variety of phospholipid monolayers using fluorescence microscopy. By labeling the enzyme with a fluorescent marker and introducing it into the subphase of a Langmuir film balance, the hydrolysis of lipid monolayers in their liquid-solid phase transition region could be directly observed with the assistance of an epifluorescence microscope. Visual observation of hydrolysis of different phospholipid monolayers in the phase transition region in real-time could differentiate various mechanisms of hydrolytic action against …

Phase transition12-DipalmitoylphosphatidylcholineStereochemistryBiophysicsPhospholipidBiochemistryPhospholipases Achemistry.chemical_compoundPhospholipase A2Phase (matter)MonolayerEnzyme StabilityFluorescence microscopeLipid bilayer phase behaviorParticle SizePhospholipidsFluorescent DyesElapid VenomsPhospholipase ABinding SitesbiologyHydrolysisPhosphatidylethanolaminesCell BiologyImage EnhancementPhospholipases A2chemistryMicroscopy FluorescencePhospholipasesBiophysicsbiology.proteinlipids (amino acids peptides and proteins)DimyristoylphosphatidylcholineBiochimica et biophysica acta
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POLYPHENOL OXIDASE ACTIVITY FROM THREE SICILIAN ARTICHOKE (CYNARA CARDUNCULUS L. VAR. SCOLYMUS L. (FIORI)) CULTIVARS: STUDIES AND TECHNOLOGICAL APPLI…

2010

Several papers helped with the development of more methods to control browning, or study thermal polyphenol oxidase (PPO) inactivation, but did not provide any solutions to technological process problems and food process improvement. Artichokes [ Cynara cardunculus L. var. scolymus L. (Fiori)] are susceptible to browning; this alteration could affect and reduce the suitability for its use, fresh or processed. Within this study, the catecholase and cresolase activities of PPO from three different Sicilian artichokes cultivar were characterized with regard to substrate specificity and enzyme kinetics, optimum pH and temperature, temperature and pH stability, and inhibitor test; all of the res…

Polyphenol oxidaseFood HandlingPolyphenol oxidaseSubstrate SpecificityCynara scolymusBotanyEnzyme StabilityBrowningCynara cardunculus L. var. scolymus L. (Fiori)CultivarCatechol oxidaseSicilyPlant ProteinsbiologyChemistryCynara scolymusCynaraTemperaturefood and beveragesGeneral Chemistrybiology.organism_classificationinhibitionHorticultureKineticsbiology.proteinPostharvestScolymusenzymatic browningGeneral Agricultural and Biological SciencesCatechol Oxidase
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The Closed/Open Model for Lipase Activation. Addressing Intermediate Active Forms of Fungal Enzymes by Trapping of Conformers in Water-Restricted Env…

2001

The behavior of prototypic fungal lipases in a water-restricted environment has been investigated by exploiting the reported experimental strategy that allows the trapping (freeze-drying) of the enzyme in the conformation present in aqueous solution and to subsequently assay it in nonaqueous media [Mingarro, I., Abad, C., and Braco, L. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 3308-3312]. We now report, using simple esterification as well as acidolysis (triglycerides as substrates) as nonaqueous model reactions, that the presence of a detergent (n-octyl-beta-glucopyranoside) in the freeze-drying buffer, at concentrations below the critical micellar concentration, generates different catalyti…

Protein ConformationStereochemistryThioglucosidesDetergentsTrappingBuffersBiochemistryFungal ProteinsAscomycotaEnzyme StabilityMoleculeLipaseConformational isomerismMicellesTriglyceridesCandidachemistry.chemical_classificationAqueous solutionbiologyWaterLipaseGeotrichumEnzyme ActivationSolutionsFreeze DryingEnzymeModels ChemicalchemistryCritical micelle concentrationbiology.proteinFungal enzymesRhizopusBiochemistry
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Strategies for the production of difficult-to-express full-length eukaryotic proteins using microbial cell factories : production of human alpha-gala…

2015

This work was supported by ERANET-IB08-007 project from the European Union and its linked national project EUI2008- 03610 to AV. We also appreciate the support from EME2007-08 to NFM from Universitat Autonoma de Barcelona, from Antartide 2010 to MLT and EP, from MIUR Azioni Integrate Italia-Spagna 2010 Prot. IT10LECLM9 to MLT, from MINECO (IT2009-0021) to AV and LT, from AGAUR (2009SGR-108) to AV. AV is also supported by The Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN, Spain), an initiative funded by the VI National R&D&i Plan 2008-2011, Iniciativa Ingenio 2010, Consolider Program, CIBER Actions and financed by the Instituto de Salud Car…

PseudoalteromonaRecombinant proteinExpression systemsFabry's diseaseHuman alpha-galactosidase AContext (language use)Computational biologyBiologymedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyPseudoalteromonas haloplanktisGene expressionEnzyme StabilitymedicineProtein biosynthesisEscherichia coliHumansEscherichia coliGenePseudoalteromonas haloplanktis TAC125Expression systemGeneral Medicinebiology.organism_classificationRecombinant ProteinsPseudoalteromonasMembrane proteinFabry’s diseaseMetabolic Engineeringalpha-GalactosidaseProtein foldingBiotechnologyHuman
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Yeast contains multiple forms of histone acetyltransferase.

1989

We have assayed several methods to quantitatively recover yeast histone acetyltransferases in an attempt to study the multiplicity of enzymatic activities. Two methods, namely (NH4)2SO4 precipitation and salt dissociation of chromatin in 0.5 M NaCl, yielded convenient preparations of total histone acetyltransferases. DEAE-Sepharose chromatography of the crude extracts resulted in the separation of three peaks of activity when total yeast histones were used as substrate. However, the scanning of the enzymatic activity toward individual histones along the chromatography, achieved by determining the specific activity of the individual histones after incubating whole histones and [14C]acetyl-Co…

Saccharomyces cerevisiae ProteinsIon chromatographySaccharomyces cerevisiaeBiochemistryHistone DeacetylasesSubstrate SpecificityHistonesAcetyltransferasesEnzyme StabilityHistone octamerMolecular BiologyHistone AcetyltransferasesHistone AcetyltransferasesChromatographybiologyChemistryAcetylationCell BiologyHistone acetyltransferaseChromatography Ion ExchangeYeastChromatinChromatinIsoenzymesKineticsHistoneBiochemistryAcetylationbiology.proteinThe Journal of biological chemistry
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Activation of protein kinase C alpha and/or epsilon enhances transcription of the human endothelial nitric oxide synthase gene.

1998

In primary human umbilical vein endothelial cells (HUVECs), incubation with phorbol-12-myristate-13-acetate (PMA) enhanced basal and bradykinin-stimulated nitric oxide production. In the HUVEC-derived cell line EA.hy 926, PMA and phorbol-12,13-dibutyrate stimulated endothelial nitric oxide synthase (NOS III) mRNA expression in a concentration- and time-dependent manner. Maximal mRNA expression (3.3-fold increase) was observed after 18 hr. NOS III protein and activity were increased to a similar extent. The specific protein kinase C (PKC) inhibitors bisindolylmaleimide I (1 microM), Gö 6976 [12-(2 cyanoethyl)-6,7,12, 13-tetrahydro-13-methyl-5-oxo-5H-indolo[2,3-a]pyrrolo-[3, 4-c]carbazole] (1…

Umbilical VeinsProtein Kinase C-alphaTime FactorsEndotheliumTranscription GeneticDown-RegulationProtein Kinase C-epsilonBiologyBradykininTransfectionNitric oxidechemistry.chemical_compoundEnzyme StabilitymedicineHumansRNA MessengerEnzyme InhibitorsProtein kinase APromoter Regions GeneticCyclic GMPProtein kinase CCells CulturedProtein Kinase CPharmacologyKinaseMethane sulfonateBiological TransportMolecular biologyUp-RegulationEnzyme ActivationIsoenzymesmedicine.anatomical_structureChelerythrinechemistryGene Expression RegulationCell cultureMolecular MedicineTetradecanoylphorbol AcetateEndothelium VascularNitric Oxide SynthaseMolecular pharmacology
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Enzymes involved in vinyl acetate decomposition by Pseudomonas fluorescens PCM 2123 strain

2014

Esterases are widely used in food processing industry, but there is little information concerning enzymes involved in decompositions of esters contributing to pollution of environment. Vinyl acetate (an ester of vinyl alcohol and acetic acid) is a representative of volatile organic compounds (VOCs) in decomposition, of which hydrolyses and oxidoreductases are mainly involved. Their activities under periodically changing conditions of environment are essential for the removal of dangerous VOCs. Esterase and alcohol/aldehyde dehydrogenase activities were determined in crude cell extract from Pseudomonas fluorescens PMC 2123 after vinyl acetate induction. All examined enzymes exhibit their hig…

Vinyl alcoholVinyl CompoundsenzymesEnzyme ActivatorsAlcoholPseudomonas fluorescensEsteraseMicrobiologyArticlechemistry.chemical_compoundAcetic acidesterasesEnzyme StabilityVinyl acetateOrganic chemistryEnzyme InhibitorsBiotransformationAlcohol dehydrogenaseEthanolbiologyAcetaldehydeTemperatureGeneral MedicineHydrogen-Ion ConcentrationKineticschemistrybiology.proteinvinyl acetateOxidoreductasesFolia Microbiologica
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