No description available.

The unscheduled formation of gas hydrate plugs in oil and gas pipelines, which can lead to serious mechanical and personnel damage, is a problematic issue in the petroleum industry. Traditionally, thermodynamic inhibitors such as methanol have been used to control the formation of gas hydrates, but due to the large expenses and ecological risks associated with its use there is increased interest in the use of alternative hydrate inhibitors. They include kinetic inhibitors (KIs) and antiagglomerants (AAs) and as their names imply, function by interfering with the kinetics of hydrate formation and hydrate agglomeration. Recently, antifreeze proteins (AFPs) have shown to inhibit hydrates and have been proposed as hydrate inhibitors. Normally, AFPs function to protect the tissues of various organisms during freezing conditions. Initially they were found in polar fish, and were later recognized in insects, plants and microorganisms. AFPs are thought to function by lowering the freezing point of water through an adsorption-inhibition mechanism. This thesis has shown that antifreeze proteins (AFPs) are able to modify the crystal morphologies of structure II (sII) tetrahydrofuran (THF) similarly to the KI poly-N-vinylpyrrolidone (PVP) by adhering to the hydrate surface and inhibiting crystal growth. The AFPs were also tested on a high-pressure sII methane/ethane/propane hydrate and proved to have superior hydrate inhibition to PVP. Yet, the expense of purifying AFPs makes them impractical for industrial purposes, thus investigations into the use of cold-adapted bacteria as hydrate inhibitors proved that isolates capable of adsorbing to THF hydrate showed the most effective THF hydrate inhibition. These findings suggest a potential for the future development of biologically-based hydrate inhibitors. / Thesis (Master, Biology) -- Queen's University, 2009-09-01 10:04:00.72

The main success of my thesis has been to establish the mechanism by which antifreeze proteins (AFPs) bind irreversibly to ice crystals, and hence prevent their growth. AFPs organize ice-like water on their ice-binding site, which then merges and freezes with the quasi-liquid layer of ice. This was revealed from studying the exceptionally large (ca. 1.5-MDa) Ca 2+-dependent AFP from the Antarctic bacterium Marinomonas primoryensis (MpAFP). The 34-kDa antifreeze- active region of MpAFP was predicted to fold as a novel Ca 2+-binding β-helix. Site-directed mutagenesis confirmed the model and demonstrated that its ice-binding site (IBS) consisted of solvent-exposed Thr and Asx parallel arrays on the Ca 2+-binding turns. The X-ray crystal structure of the antifreeze region was solved to a resolution of 1.7 Å. Two of the four molecules within the unit cell of the crystal had portions of their IBSs freely exposed to solvent. Identical clathrate-like cages of water molecules were present on each IBS. These waters were organized by the hydrophobic effect and anchored to the protein via hydrogen bonds. They matched the spacing of water molecules in an ice lattice, demonstrating that anchored clathrate waters bind AFPs to ice. This mechanism was extended to other AFPs including the globular type III AFP from fishes. Site-directed mutagenesis and a modified ice-etching technique demonstrated this protein uses a compound ice-binding site, comprised of two flat and relatively hydrophobic surfaces, to bind at least two planes of ice. Reinvestigation of several crystal structures of type III AFP identified anchored clathrate waters on the solvent-exposed portion of its compound IBS that matched the spacing of waters on the primary prism plane of ice. Ice nucleation proteins (INPs), which can raise the temperature at which ice forms in solution to just slightly below 0oC, have the opposite effect to AFPs. A novel dimeric β-helical model was proposed for the INP produced by the bacterium Pseudomonas borealis. Molecular dynamics simulations showed that INPs are also capable of ordering water molecules into an ice- like lattice. However, their multimerization brings together sufficient ordered waters to form an ice nucleus and initiate freezing. / Thesis (Ph.D, Biochemistry) -- Queen's University, 2011-08-08 14:09:05.143

The formation of gas hydrates in the oil and gas industry causes numerous problems that require costly solutions and operation downtime. A great deal of hydrate research has focused on their prevention either through kinetic or thermodynamic inhibitors. Recently, antifreeze proteins (AFPs) produced by cold adapted organisms have been found to have a kinetic inhibitory effect on clathrate hydrates. / Kinetic experiments were conducted on the methane-water system in the presence of AFPs by measuring the gas uptake during the formation of methane hydrate in a 610 cc high pressure crystallizer. These experiments were performed at temperatures ranging from 277.15 K to 280.65 K, pressures of 5800 KPa to 8100 KPa and at an AFP concentration of 0.01 mM. / The results of these experiments showed that the presence of AFPs affect methane hydrate formation in multiple ways. They were shown to increase the nucleation time, reduce the initial growth rate of methane hydrate at the time of nucleation and there was evidence to suggest that they also have an anti-agglomerating effect on hydrate crystals.

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Thesis (M.S.)--Ohio University, November, 2007. / Title from PDF t.p. Includes bibliographical references.

Thesis (M.Eng.). / Written for the Dept. of Chemical Engineering. Title from title page of PDF (viewed 2008/01/14). Includes bibliographical references.

Thesis (Ph. D.)--State University of New York at Binghamton, Department of Chemistry, 2004. / Includes bibliographical references.

Thesis (M.Sc.)--Memorial University of Newfoundland, 2005. / Bibliography: leaves 62-68.

Thesis (Ph. D.)--State University of New York at Binghamton, Chemistry Department, 2004. / Includes bibliographical references.