Search results for "Enzyme Stability"

showing 7 items of 37 documents

Rational backbone redesign of a fructosyl peptide oxidase to widen its active site access tunnel

2020

Fructosyl peptide oxidases (FPOXs) are enzymes currently used in enzymatic assays to measure the concentration of glycated hemoglobin and albumin in blood samples, which serve as biomarkers of diabetes. However, since FPOX are unable to work directly on glycated proteins, current enzymatic assays are based on a preliminary proteolytic digestion of the target proteins. Herein, to improve the speed and costs of the enzymatic assays for diabetes testing, we applied a rational design approach to engineer a novel enzyme with a wider access tunnel to the catalytic site, using a combination of Rosetta design and molecular dynamics simulations. Our final design, L3_35A, shows a significantly wider …

access tunnel biosensor diabetes fructosyl peptide oxidase rational enzyme designBioengineeringPeptidebiosensorApplied Microbiology and Biotechnologychemistry.chemical_compoundCatalytic DomainEnzyme Stabilityfructosyl peptide oxidasechemistry.chemical_classificationdiabetesbiologyPoint mutationRational designProteolytic enzymesAlbuminActive siteSettore CHIM/08 - Chimica FarmaceuticaEnzymeBiochemistrychemistryrational enzyme designbiology.proteinAmino Acid OxidoreductasesGlycated hemoglobinaccess tunnelBiotechnology
researchProduct

Ability of Kocuria varians LTH 1540 To Degrade Putrescine: Identification and Characterization of a Novel Amine Oxidase.

2015

This work describes the identification and characterization of an amine oxidase from Kocuria varians LTH 1540 (syn. Micrococcus varians) primarily acting on putrescine. Data from MALDI-TOF MS/MS and the identification of Δ(1)-pyrroline as degradation product from putrescine indicate that the enzyme is a flavin-dependent putrescine oxidase (PuO). Properties of partially purified enzyme have been determined. The enzyme oxidizes diamines, putrescine and cadaverine, and, to a lesser extent, polyamines, such as spermidine, but not monoamines. The kinetic constants (Km and Vmax) for the two major substrates were 94 ± 10 μM and 2.3 ± 0.1 μmol/min·mg for putrescine and 75 ± 5 μM and 0.15 ± 0.02 μmo…

chemistry.chemical_classificationAmine oxidaseCadaverineOxidoreductases Acting on CH-NH Group DonorsChromatographyKocuria variansGeneral ChemistryBiologyHydrogen-Ion ConcentrationAmine oxidase inhibitorsMicrococcusSpermidinePutrescine oxidasechemistry.chemical_compoundKineticsEnzymeBiodegradation EnvironmentalchemistryBacterial ProteinsEnzyme StabilityPutrescinePutrescineGeneral Agricultural and Biological SciencesJournal of agricultural and food chemistry
researchProduct

Biochemical characterization of two functional human liver acyl-CoA oxidase isoforms 1a and 1b encoded by a single gene

2007

Abstract Human acyl-CoA oxidase 1 (ACOX1) is a rate-limiting enzyme in peroxisomal fatty acids β-oxidation and its deficiency is associated with a lethal, autosomal recessive disease, called pseudoneonatal-adrenoleukodystrophy. Two mRNA variants, transcribed from a single gene encode ACOX1a or ACOX1b isoforms, respectively. Recently, a mutation in a splice site has been reported [H. Rosewich, H.R. Waterham, R.J. Wanders, S. Ferdinandusse, M. Henneke, D. Hunneman, J. Gartner, Pitfall in metabolic screening in a patient with fatal peroxisomal β-oxidation defect, Neuropediatrics 37 (2006) 95–98.], which results in the defective peroxisomal fatty acids β-oxidation. Here, we show that these mRNA…

chemistry.chemical_classificationGene isoformOxidase testBiophysicsCell BiologyBiologyPeroxisomeBiochemistryIsozymeMolecular biologyArticleEnzyme ActivationIsoenzymesMolecular WeightEnzymechemistryBiochemistryLiverEnzyme StabilityAcyl-CoA oxidaseACOX1HumansHeterologous expressionAcyl-CoA OxidaseMolecular Biology
researchProduct

Calculation of the molecular masses of two newly synthesized thermostable enzymes isolated from thermophilic microorganisms

1995

Two thermostable enzymes synthesized by thermophilic microorganisms were isolated and purified. A thermostable beta-galactosidase was produced in a continuous fermentation process by Bacillus stearothermophilus TP 32 as an intracellular enzyme. After applying different concentration procedures the raw extract enzyme was prepurified on a Sephadex G-200 size exclusion column. The isolated beta-galactosidase fraction was then separated with HPLC on a TSK G 3000 SW size exclusion column to determine the molecular mass based on calibration curves of standard proteins. The other enzyme, a thermostable protease, was synthesized by Bacillus stearothermophilus TP 26 as an extracellular enzyme. After…

chemistry.chemical_classificationHot TemperatureProteaseChromatographybiologyMolecular massmedicine.medical_treatmentThermophileSize-exclusion chromatographyGeneral Chemistrybeta-Galactosidasebiology.organism_classificationBacillalesHigh-performance liquid chromatographyGeobacillus stearothermophilusMolecular WeightEnzymechemistrySephadexEndopeptidasesEnzyme StabilityChromatography GelmedicineChromatography High Pressure LiquidJournal of Chromatography B: Biomedical Sciences and Applications
researchProduct

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
researchProduct

Recent advances in the application of microbial transglutaminase crosslinking in cheese and ice cream products: A review

2018

Microbial transglutaminase (MTGase) has been currently utilized to form new food structures and matrices with high physicochemical stability. Incorporation of this multi-functional enzyme into structural composition of milk protein-based products, such as cheese and ice cream, can not only be a successful strategy to improve their nutritional and technological characteristics through intramolecular cross-linking, but also to reduce the production cost by decreasing fat and stabilizer contents. The recent research developments and promising results of MTGase application in producing functional formulations of cheese and ice cream with higher quality characteristics are reviewed. New interest…

food.ingredientFood HandlingOrganolepticBiochemistry0404 agricultural biotechnologyfoodCheeseStructural BiologyEnzyme StabilityAnimalsHumans[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringFood scienceMolecular Biology2. Zero hungerTransglutaminasesMoisture[SDE.IE]Environmental Sciences/Environmental EngineeringChemistryIce CreamFood additivefood and beveragesFood composition data04 agricultural and veterinary sciencesGeneral MedicineMilk Proteins040401 food scienceCross-Linking ReagentsWhey ProteinsIce creamFood TechnologyFood qualityMicrobial transglutaminaseStabilizer (chemistry)International Journal of Biological Macromolecules
researchProduct

Tartrate-Resistant Acid Phosphatase 5b: A Novel Serum Marker of Bone Resorption

2000

Human serum contains two forms of tartrate-resistant acid phosphatase (TRAP), 5a and 5b. Of these, 5a contains sialic acid and 5b does not. We show here that antigenic properties and pH optimum of TRAP purified from human osteoclasts are identical to those of serum TRAP 5b and completely different from those of serum TRAP 5a, suggesting that 5b would be derived from osteoclasts and 5a from some other source. We developed a novel immunoassay specific for 5b using a monoclonal antibody O1A as capture antibody. O1A did not bind acid phosphatase derived from platelets and erythrocytes. Western analysis showed that O1A was specific for TRAP in both human bone and serum. We measured bound TRAP ac…

medicine.medical_specialtyEndocrinology Diabetes and MetabolismAcid PhosphataseNeuraminidaseBone resorptionPlaceboschemistry.chemical_compoundDouble-Blind MethodReference ValuesOsteoclastInternal medicineEnzyme StabilitymedicineHumansOrthopedics and Sports MedicineBone ResorptionIncubationTartrate-resistant acid phosphataseEstradiolmedicine.diagnostic_testbiologyTartrate-Resistant Acid PhosphataseEstrogen Replacement TherapyAcid phosphataseAntibodies MonoclonalMiddle AgedSialic acidResorptionIsoenzymesPostmenopauseEndocrinologymedicine.anatomical_structurechemistryImmunoassaybiology.proteinFemaleNorethindroneBiomarkersJournal of Bone and Mineral Research
researchProduct