Search results for "BIOTRANSFORMATION"

showing 10 items of 183 documents

Use of Saccharomyces cerevisiae as a whole cell system for aldol condensation in organic medium: Study of the factors affecting the biotransformation

2011

Abstract Saccharomyces cerevisiae has been employed as a whole cell catalyst for a number of asymmetric transformations. This work explores the ability of this microorganism to carry out the asymmetric aldol condensation between 4-nitrobenzaldehyde and acetone. For this purpose, lyophilized cells of the FY86 laboratory strain from stationary phase cultures were employed. This reaction shows stereoselectivity, and its progress is affected by the water concentration in the medium, temperature and the growth stage of the yeast culture. Cell lysis experiments indicate that activity responsible for this biotransformation is located in the soluble fraction.

LysisbiologyChemistryProcess Chemistry and TechnologyMicroorganismSaccharomyces cerevisiaeBioengineeringbiology.organism_classificationBiochemistryCatalysisYeastchemistry.chemical_compoundBiotransformationAcetoneOrganic chemistryAldol condensationStereoselectivityJournal of Molecular Catalysis B: Enzymatic
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Peroxisomal beta-oxidation activities and gamma-decalactone production by the yeast Yarrowia lipolytica.

1998

International audience; gamma-Decalactone is a peachy aroma compound resulting from the peroxisomal beta-oxidation of ricinoleic acid by yeasts. The expression levels of acyl-CoA oxidase (gene deletion) and 3-ketoacyl-CoA thiolase activities (gene amplification on replicative plasmids) were modified in the yeast Yarrowia lipolytica. The effects of these modifications on beta-oxidation were measured. Overexpression of thiolase activity did not have any effect on the overall beta-oxidation activity. The disruption of one of the acyl-CoA oxidase genes resulted in an enhanced activity. The enhancement led to an increase of overall beta-oxidation activity but reduced the gamma-decalactone produc…

MESH: Oxidation-ReductionRicinoleic acidMESH: MicrobodiesMicrobodiesApplied Microbiology and BiotechnologyAROME DE PECHELactoneschemistry.chemical_compoundMESH : BiotransformationYeastsMESH : Microbodies[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAcyl-CoA oxidaseMESH: Blotting NorthernNorthern[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology[INFO.INFO-BT]Computer Science [cs]/Biotechnology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyBiotransformationMESH : Oxidation-ReductionMESH: BiotransformationMESH : YeastsOxidase testbiologyBlottingCatabolismThiolaseMESH: YeastsMESH : Blotting NorthernYarrowiaGeneral MedicinePeroxisomeBlotting Northernbiology.organism_classificationYeastMESH : LactonesMESH: Ricinoleic Acids[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology[INFO.INFO-BT] Computer Science [cs]/BiotechnologyBiochemistrychemistryMESH : Ricinoleic AcidsACYL COA OXYDASERicinoleic AcidsOxidation-Reduction[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyMESH: LactonesBiotechnology
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Direct and indirect measurements of enhanced phenolic bioavailability from litchi pericarp procyanidins by Lactobacillus casei-01

2017

Litchi pericarp procyanidins (LPP) are dietary supplements with high antioxidant activity, but poor oral bioavailability and efficacy. Lactobacillus casei (L. casei-01) can transform flavan-3-ols from litchi pericarp and increase their antioxidant ability; thus, L. casei-01 with LPP was administered to rats for four and eight weeks to study the effect of such a combination on metabolic parameters and on phase II metabolism and detoxification pathways in the liver as an indirect measure for phenolic bioavailability. Our data indicated that the T-AOC of the plasma, the liver GSH-Px and GSH-ST activity, and the expression of UGT and SULT isoforms in the liver of the rats were all enhanced afte…

Male0301 basic medicineURINARY-EXCRETIONAntioxidantmedicine.medical_treatmentCHINENSIS PERICARPCatechinRats Sprague-DawleyBiotransformationIngestionFood scienceBiotransformationGENE-EXPRESSIONGlutathione TransferasebiologyChemistryfood and beverages04 agricultural and veterinary sciencesGeneral Medicine040401 food scienceLacticaseibacillus caseiLiverBiochemistryUDP-GLUCURONOSYLTRANSFERASE; PROTEASOMAL DEGRADATION; ANTIOXIDANT ACTIVITY; PROBIOTIC BACTERIA; CHINENSIS PERICARP; URINARY-EXCRETION; GENE-EXPRESSION; IN-VITRO; NRF2; POLYPHENOLSPROTEASOMAL DEGRADATIONPROBIOTIC BACTERIALactobacillus caseiAbsorption (skin)NRF203 medical and health sciencesPOLYPHENOLS0404 agricultural biotechnologyLitchiPhenolsDetoxificationmedicineAnimalsBiflavonoidsProanthocyanidinsGlutathione PeroxidasePlant ExtractsUDP-GLUCURONOSYLTRANSFERASEIN-VITRObiology.organism_classificationRatsBioavailabilitybody regionsTransformation (genetics)030104 developmental biologyFruitANTIOXIDANT ACTIVITYFood ScienceFood & Function
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Rat liver endothelial and Kupffer cell-mediated mutagenicity of polycyclic aromatic hydrocarbons and aflatoxin B1.

1990

The ability of isolated rat liver endothelial and Kupffer cells to activate benzo(a)pyrene (BP), trans-7,8-dihydroxy-7,8-dihydrobenzo(a)pyrene (DDBP), trans-1,2-dihydroxy-1,2-dihydrochrysene (DDCH), and aflatoxin B1 (AFB1) to mutagenic metabolites was assessed by means of a cell-mediated bacterial mutagenicity assay and compared with the ability of parenchymal cells to activate these compounds. Endothelial and Kupffer cells from untreated rats were able to activate AFB1 and DDBP; DDBP was activated even in the absence of an NADPH-generating system. Pretreating the animals with Aroclor 1254 strongly enhanced the mutagenicity of the dihydrodiol, whereas the mutagenicity of AFB1 showed a sligh…

MaleAflatoxin B1EndotheliumKupffer CellsLiver cytologyHealth Toxicology and MutagenesisIn Vitro TechniquesBiologychemistry.chemical_compoundAflatoxinsmedicineOrganoidAnimalsPolycyclic CompoundsTestosteroneBiotransformationCarcinogenKupffer cellPublic Health Environmental and Occupational Healthfood and beveragesRats Inbred StrainsRatsmedicine.anatomical_structureLiverBiochemistrychemistryBenzopyreneToxicityMicrosomeEndothelium VascularResearch ArticleMutagensEnvironmental Health Perspectives
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DNA binding, adduct characterisation and metabolic activation of aflatoxin B1 catalysed by isolated rat liver parenchymal, Kupffer and endothelial ce…

1991

In vitro studies with rat liver parenchymal, Kupffer and endothelial cells isolated from male Sprague-Dawley rats were undertaken to investigate cell-specific bioactivation of aflatoxin B1, DNA binding and adduct formation. In the mutagenicity studies, using homogenates of all three separated liver cell populations (co-incubated with NADP+ and glucose-6-phosphate as cofactors for the cytochrome P-450 monooxygenase system) parenchymal, Kupffer and endothelial cells were able to activate aflatoxin B1 to a metabolite mutagenic to Salmonella typhimurium TA 98. In the case of nonparenchymal cells (i.e. Kupffer and endothelial cells) 10-fold higher concentrations of aflatoxin B1 had to be used to…

MaleAflatoxinAroclorsAflatoxin B1Kupffer CellsHealth Toxicology and MutagenesisMetaboliteBiologyIn Vitro TechniquesToxicologychemistry.chemical_compoundmedicineAnimalsTestosteroneEndotheliumBiotransformationMutagenicity TestsLiver cellKupffer cellfood and beveragesRats Inbred StrainsGeneral MedicineDNAMonooxygenaseChlorodiphenyl (54% Chlorine)In vitroRatsEndothelial stem cellmedicine.anatomical_structurechemistryBiochemistryLiverMicrosomeArchives of toxicology
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Reductive and oxidative metabolism of nitrofurantoin in rat liver.

1980

The elimination of nitrofurantoin was studied in the isolated rat liver using a recirculating hemoglobin-free perfusion system. The most rapid clearance of nitrofurantoin (0.1 mM) was found under hypoxia (8 ml/min) or anoxia (11 ml/min) indicating a fast and oxygen-sensitive reductive metabolism. The hepatic elimination of nitrofurantoin under anaerobic conditions apparently is not catalyzed by xanthine oxidase, aldehyde oxidase or cytochrome P-450 as judged from the lack of influence of the inhibitors (0.1 mM) allopurinol, menadione, metyrapone, α-naphthoflavone or of carbon monoxide (50%; v/v). Under aerobic conditions the hepatic clearance of nitrofurantoin is rather low (1 ml/min) indic…

MaleAllopurinolPharmacologyIn Vitro Techniquesurologic and male genital diseasesHydroxylationchemistry.chemical_compoundOxygen ConsumptionMenadionemedicineAnimalsXanthine oxidaseAldehyde oxidaseBiotransformationPharmacologyChemistryGeneral MedicineMetabolismfemale genital diseases and pregnancy complicationsRatsBiochemistryLiverNitrofurantoinNitrofurantoinMicrosomeOxidation-Reductionmedicine.drugSubcellular FractionsNaunyn-Schmiedeberg's archives of pharmacology
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Novel Antihypertensive Lactoferrin-Derived Peptides Produced by Kluyveromyces marxianus: Gastrointestinal Stability Profile and In Vivo Angiotensin I…

2014

Novel antihypertensive peptides released by Kluyveromyces marxianus from bovine lactoferrin (LF) have been identified. K. marxianus LF permeate was fractionated by semipreparative high performance liquid chromatography and 35 peptides contained in the angiotensin I-converting enzyme (ACE)-inhibitory fractions were identified by using an ion trap mass spectrometer. On the basis of peptide abundance and common structural features, six peptides were chemically synthesized. Four of them (DPYKLRP, PYKLRP, YKLRP, and GILRP) exerted in vitro inhibitory effects on ACE activity and effectively decreased systolic blood pressure after oral administration to spontaneously hypertensive rats (SHRs). Stab…

MaleAntihypertensive effectsAdministration OralAngiotensin-Converting Enzyme InhibitorsBlood PressurePeptideLactoferrin-derived peptidesPeptidyl-Dipeptidase AKluyveromycesKluyveromyces marxianusIn vivoRats Inbred SHRRenin–angiotensin systemAnimalsHumansKluyveromyces marxianusAmino Acid SequencePeptide sequenceAntihypertensive AgentsBiotransformationchemistry.chemical_classificationbiologyLactoferrinGastrointestinal digestionGeneral Chemistrybiology.organism_classificationAngiotensin IIRatsLactoferrinEnzymeBiochemistrychemistryHypertensionbiology.proteinCattlePeptidesGeneral Agricultural and Biological SciencesIn vivo ACE inhibition
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Large differences in metabolic activation and inactivation of chemically closely related compounds: effects of pure enzymes and enzyme induction on t…

1981

MaleAroclorsCancer ResearchAmes testMicechemistry.chemical_compoundBenz(a)AnthracenesmedicineAnimalsBenz(a)AnthracenesEnzyme inducerBiotransformationEpoxide Hydrolaseschemistry.chemical_classificationMice Inbred C3HbiologyMutagenicity TestsChemistry712-Dimethylbenz[a]anthraceneGeneral MedicineChlorodiphenyl (54% Chlorine)EnzymesCytosolEnzymeBiochemistryEnzyme InductionPhenobarbitalbiology.proteinPhenobarbitalDihydrodiol dehydrogenaseMethylcholanthreneMutagensmedicine.drugCarcinogenesis
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Metabolic Activation of the (+)-S,S- and (−)-R,R-Enantiomers of trans-11,12-Dihydroxy-11,12-dihydrodibenzo[a,l]pyrene:  Stereoselectivity, DNA Adduct…

1997

Polycyclic aromatic hydrocarbons require metabolic activation in order to exert their biological activity initiated by DNA binding. The metabolic pathway leading to bay or fjord region dihydrodiol epoxides as ultimate mutagenic and/or carcinogenic metabolites is thought to play a dominant role. For dibenzo[a,l]pyrene, considered as the most potent carcinogenic polycyclic aromatic hydrocarbon, the formation of the fjord region syn- and/or anti-11,12-dihydrodiol 13,-14-epoxide (DB[a,l]PDE) diastereomers has been found to be the principal metabolic activation pathway in cell cultures leading to DNA adducts. In order to further elucidate the stereoselectivity involved in this activation pathway…

MaleAroclorsStereochemistryToxicologyChinese hamsterDihydroxydihydrobenzopyrenesRats Sprague-DawleyDNA AdductsMicechemistry.chemical_compoundCricetulusCricetinaepolycyclic compoundsAnimalsBiotransformationCarcinogenchemistry.chemical_classificationCarcinogenic Polycyclic Aromatic HydrocarbonbiologyStereoisomerismGeneral MedicineChlorodiphenyl (54% Chlorine)biology.organism_classificationRatsMetabolic pathwayEnzymechemistryCarcinogensMicrosomes LiverMicrosomePyreneStereoselectivityMutagensChemical Research in Toxicology
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Characterization of DNA adducts at the bay region of dibenz[a,h]anthracene formed in vitro

1993

Bay region diolepoxide-DNA adducts of dibenz[a,h]anthracene (DBA) formed in vitro were identified and their absolute stereochemistry was assigned. After activation of [5,12-14C]DBA with liver microsomes obtained from Aroclor 1254 treated male Sprague-Dawley rats in the presence of calf thymus DNA for 1 h, the amount of DNA adducts was found to be 9.9 +/- 2.4 pmol/mg DNA, calculated on the basis of the portion of radioactivity eluted from the HPLC reversed-phase column with a water/acetonitrile gradient. Bay region diolepoxide-DNA adducts represented 27.5% of radioactivity associated with DNA adducts. The absolute configuration of the various adducts was determined from the reaction of the (…

MaleCancer ResearchAnthraceneMetaboliteAbsolute configurationStereoisomerismDNAGeneral MedicineIn Vitro TechniquesHigh-performance liquid chromatographyMedicinal chemistryRatsAdductRats Sprague-DawleyDNA Adductschemistry.chemical_compoundchemistryBiochemistryDeoxyadenosineBenz(a)AnthracenesMicrosomes LiverAnimalsDeoxyguanosineDibenz(ah)anthraceneBiotransformationCarcinogenesis
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