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Showing 1 to 13 of 13 for “"enzyme inactivation"”.
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A comparison among lipoxygenase, trypsin inhibitor, and urease enzyme inactivation during blanching of dehulled and whole soybeans
This study investigated the thermal inactivation by immersion cooking of antinutritional factors in soybeans while minimizing protein insolubilization. The comparison of inactivation kinetics of lipoxygenase (LO), trypsin inhibitors (TI), and urease (U) enzyme was used to determine the limiting …
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The Roles of Peroxynitrite and Superoxide in Oxidative Damage to E. Coli
… intracellular targets as superoxide. Of nineteen enzymes tested, only the dehydratase enzymes containing these iron-sulfur clusters were significantly affected by peroxynitrite challenge. These iron-sulfur clusters could be repaired, and both iron storage proteins and iron import seem to be …
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Application of additives in horseradish peroxidase-catalyzed removal of phenol derivatives from aqueous solution.
… of phenolic compounds to increase the enzyme turnovers by more than 100-fold. In addition to polyethylene glycol (PEG) and gelatin, some polyelectrolytes may also prove effective as additives. The HRP saving is contingent on the nature of the additives and phenolic compounds. PEG …
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Application of the extended Kalman filter to enzyme reactions
… to a biological problem, we used two different enzyme reactions as model systems. The first model problem is a simulation of cellulose hydrolysis with enzyme inactivation. The second model problem is a simulation of the separation of a chiral substance into its respective enantiomers. In the …
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Investigations of the inhibition mechanisms of human ribonucleotide reductase by gemcitabine-5'-diphosphate and saccharomyces cerevisiae ribonucleotide reductase by Sml1
… and the phosphorylated F2C targets many enzymes involved in nucleotide metabolism, including RNR. The studies presented here with [1 '-3H]- and [5- 3H]-F 2CDP have established that F2CDP is a sub-stoichiometric mechanism based inhibitor (0.5 equivalents F2CDP/[alpha]) of both the E. coli …
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Controlling the Stability of Colloidal Drug Aggregates for Chemotherapeutic Delivery
… results in screening assays. In biochemical enzyme inhibition assays colloids non-specifically adsorb proteins leading to partial unfolding and enzyme inactivation. In cell-based cytotoxicity assays colloids are unable to cross cell membranes leading to the drug being unable to bind to its …
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Participation of the iron-sulfur cluster of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase in the inactivation and degradation of the enzyme in vivo
… cluster which is essential for activity. The enzyme also undergoes removal of 11 N-terminal residues from the primary translation product in vivo to form the active enzyme. It has been proposed that oxidative inactivation of the FeS cluster in vivo is the first step in degradation of the …
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Halo Enol Lactones as Enzyme-Activated Irreversible Inhibitors of Chymotrypsin: Their Synthesis, Kinetics, and Mechanism of Inactivation (Suicide Substrates)
Halo enol lactones can act as enzyme-activated irreversible inhibitors or suicide substrates for (alpha)-chymotrypsin. Acyl transfer to the active site serine generates a halo methyl ketone that remains tethered in the catalytic site during the lifetime of the acyl enzyme, available for reaction …
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Using Esterase and Laccase Enzymes to Derivatize Bioactive Plant Phenolics for Altered Chemistry
… their action by chemical modification. Two enzyme classes carry out reactions that can act on the hydroxyl moiety of phenolics. Esterase enzymes can be used in non-aqueous solvents to esterify a long chain acyl group onto the phenolic compound. Laccase enzymes can be used to form phenoxy …
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Fundamental phenomenological description and experimental optimization of gel stabilized biocatalysts in a two-phase system
… involved in this phenomena. Localisation of the enzyme active sites in the hydrogel is performed via the synthesis of an amphiphilic phosphonate inhibitor (n-dodecyl, n-paranitrophenyl, n-hexylphosphonate) leading to limit the enzymatic activity at the alginate/hexane interface. Dissociation of …
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Stability of microbial transglutaminase and its reactions with individual caseins under atmospheric and high pressure
Kinetic inactivation of factor XIIIa and MTG were performed in a pressure range from 0.1 to 400 MPa at 40°C within a time from 0 to 60 min in a TRIS-acetate buffer at pH 6.0. The inactivation of both enzymes at these conditions followed a first order reaction model. The high inactivation rate …
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Study of non-thermal technologies to preserve the quality of fresh foods
La preocupación por consumir productos más saludables, con aspecto natural y mínimamente procesados ha aumentado notablemente. Con el fin de asegurar la seguridad de un alimento, la técnica habitual es el tratamiento térmico, pero esto conlleva una pérdida de nutrientes y de calidad. Es necesario …
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Development of a New Class of Viral Disinfectants: Enzymatic Inactivation of Sa-11 Rotavirus
… at 25°C, and pH 8.5 in 3 days, indicating that enzymes were relatively effective at lower temperatures. SA-11 rotavirus virus was then tested for sensitivity to pH at 25°C and 15°C in absence of enzyme. At pH 2, 25°C a ~4 log reduction was seen following 15 min of treatment, with viable virus …