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The effect of protein structural configuration on the free enzyme kinetic behavior of urease /

Current enzyme kinetic equations are inadequate for modelling enzymatic reactor systems because they fail to take into account the interactions between that various process parameters. They also are unable to predict reaction rates in complex solute systems. A quasi-native kinetic model was developed that predicts enzyme activity by examining the effect of solute addition on the overall protein structure. The theory was tested using the enzyme urease (urea aminohydrolase EC 3.5.1.5). / The quasi-native model was found to accurately predict both the activation and inhibition phenomena observed with urease and could also predict enzymatic activity in complex solute systems. The quasi-native isomerization constant was shown to be a function of hydrophobic effects characterized by the Sechenov theory and electrostatic effects characterized by the DeBye-Huckel theory. The Sechenov constant was found to be independent of temperature and pH. / The urease denaturation rate constant displayed a response to solute addition similar to that observed with the quasi-native isomerization equilibrium constant. However, the effect of pH on urease kinetics was a complex function of the ionization of active-site ligands and enzyme surface charge interactions.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.75699
Date January 1987
CreatorsLencki, Robert W. J.
ContributorsNeufeld, R. J. (advisor)
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageDoctor of Philosophy (Department of Chemical Engineering.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 000665172, proquestno: AAINL46072, Theses scanned by UMI/ProQuest.

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