Search results for "Pyrococcus furiosus"

showing 3 items of 3 documents

Revalorization of cellulosic wastes from Posidonia oceanica and Arundo donax as catalytic materials based on affinity immobilization of an engineered…

2020

Catalytic materials obtained by enzyme immobilization have multiple potential applications in the food industry. The choice of the immobilization method and support may be critical to define the properties of the immobilized enzyme compared to the soluble form. Although the use of immobilized enzymes shows multiple advantages, their catalytic efficiency is compromised in many instances. Molecular engineering techniques have been used to generate hybrid proteins where the enzyme of interest is fused to a module with affinity to a specific biopolymer. Binding of the hybrid TmLac-CBM2 protein, in which the β-galactosidase from Thermotoga maritima is fused to a carbohydrate-binding module from …

Immobilized enzymeGeneral Chemical Engineeringengineering.material01 natural sciencesHydrolysischemistry.chemical_compound0404 agricultural biotechnology0103 physical sciencesOrganic chemistryHemicelluloseCelluloseCelluloseCarbohydrate-binding moduleLactaseBioaffinity-based immobilization010304 chemical physicsbiology04 agricultural and veterinary sciencesGeneral ChemistryEnzyme bioadsorptionbiology.organism_classification040401 food scienceHemicellulosechemistryCellulosic ethanolengineeringPyrococcus furiosusCarbohydrate-binding moduleBiopolymerFood Science
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Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

2017

The human chaperonin complex is a ~ 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy in humans. In previous work, we introduced an equivalent mutation in an archaeal chaperonin that assembles into two octameric rings like in humans but in which all subunits are identical. We reported that the hexadecamer formed by the mutant subunit is unstable with impaired chaperoning functions. This study quantifies the loss of structural stability in the hexadecamer due to the pathogenic mutation, using differential scanning calorim…

0301 basic medicineProtein subunitMutantBiophysicsHeterologousBiochemistryChaperoninChaperoninlcsh:Biochemistry03 medical and health sciencesDSC differential scanning calorimetryCCT% chaperoninPf Pyrococcus furiosusDenaturation (biochemistry)lcsh:QD415-436Molecular Biologylcsh:QH301-705.5DLS dynamic light scatteringbiologyITC isothermal titration calorimetryWild typeIsothermal titration calorimetryCell BiologyChaperonopathiesbiology.organism_classificationProtein calorimetryNeuropathyPyrococcus furiosus030104 developmental biologyBiochemistryBiophysiclcsh:Biology (General)Pyrococcus furiosusChaperonopathieCCT5; Chaperonin; Chaperonopathies; Neuropathy; Protein calorimetry; Pyrococcus furiosus; Biophysics; Biochemistry; Molecular Biology; Cell BiologyCCT5Pyrococcus furiosuResearch ArticlePf-CD1 Pyrococcus furiosus chaperonin subunit with the last 22 amino acids deletedBiochemistry and Biophysics Reports
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Development of enzymatically-active bacterial cellulose membranes through stable immobilization of an engineered beta-galactosidase

2018

Enzymatically-active bacterial cellulose (BC) was prepared by non-covalent immobilization of a hybrid enzyme composed by a β-galactosidase from Thermotoga maritima (TmLac) and a carbohydrate binding module (CBM2) from Pyrococcus furiosus. TmLac-CBM2 protein was bound to BC, with higher affinity at pH 6.5 than at pH 8.5 and with high specificity compared to the non-engineered enzyme. Both hydrated (HBC) and freeze-dried (DBC) bacterial cellulose showed equivalent enzyme binding efficiencies. Initial reaction rate of HBC-bound enzyme was higher than DBC-bound and both of them were lower than the free enzyme. However, enzyme performance was similar in all three cases for the hydrolysis of 5% l…

0301 basic medicineImmobilized enzyme02 engineering and technologyProtein EngineeringBiochemistryBacterial cellulose03 medical and health sciencesHydrolysischemistry.chemical_compoundCarbohydrate binding moduleStructural BiologyEnzyme StabilityThermotoga maritimaCelluloseMolecular BiologyLactasechemistry.chemical_classificationbiologyGluconacetobacter xylinusHydrolysisMembranes ArtificialGeneral Medicine021001 nanoscience & nanotechnologybiology.organism_classificationEnzymes Immobilizedbeta-GalactosidaseEnzyme binding030104 developmental biologyEnzymeProtein immobilizationchemistryBiochemistryBacterial celluloseThermotoga maritimaPyrococcus furiosusCarbohydrate-binding module0210 nano-technology
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