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mso-tstyle-colband-size:0 / mso-style-noshow:yes / mso-style-priority:99 / mso-style-parent:"" / mso-padding-alt:0cm 5.4pt 0cm 5.4pt / mso-para-margin-top:0cm / mso-para-margin-right:0cm / mso-para-margin-bottom:10.0pt / mso-para-margin-left:0cm / line-height:115% / mso-pagination:widow-orphan / font-size:11.0pt / font-family:"Calibri","sans-serif" / mso-ascii-font-family:Calibri / mso-ascii-theme-font:minor-latin / mso-hansi-font-family:Calibri / mso-hansi-theme-font:minor-latin / mso-bidi-font-family:"Times New Roman" / mso-bidi-theme-font:minor-bidi / mso-fareast-language:EN-US / } </style> <![endif]--> <p style="margin-bottom:0cm / margin-bottom:.0001pt / text-align: justify / line-height:normal / mso-layout-grid-align:none / text-autospace:none" class="MsoNormal"><span style="font-size:10.0pt / font-family:&quot / Arial&quot / ,&quot / sans-serif&quot / ">There has been a decline in the global fossil fuel reserves, due to an increasing demand for petroleum. Biofuels can be used as an alternative source of energy whereby biomass is converted to liquid fuels such as bioethanol. There is considerable interest in lipolytic enzymes because of their broad substrate range and for this purpose these enzymes have potential in a variety of biotechnological application. Lipolytic enzymes include esterases (E.C 3.1.1.1) and lipases (E.C3.1.1.3). Esterases preferentially hydrolyse short chain (&lt / C10) ester-containing molecules that are partly soluble in water, while lipases hydrolyse a broad range of substrates preferably water-insoluble fatty acyl molecules (&gt / C10). The aim of this study was to express, purify and characterise the lipolytic enzyme present on afosmid, Try 11, previously isolated from a metagenomic library of a Malawian hotspring, which conferred activity on tributyrin and ethyl ferulate. Bioinformatic analysisof the fosmid insert sequence predicted an open reading frame consisting of 951 bp,designated RHgene34, encoding a 317 amino acid protein with 41 % similarity to the</span><span style="font-size: 10.0pt / font-family:&quot / Arial&quot / ,&quot / sans-serif&quot / mso-fareast-font-family:ArialOOEnc">&alpha / /&beta / hydrolase fold-3 domain protein of </span><i><span style="font-size:10.0pt / font-family:&quot / Arial&quot / ,&quot / sans-serif&quot / ">Burkholderia </span></i><span style="font-size:10.0pt / font-family:&quot / Arial&quot / ,&quot / sans-serif&quot / ">sp. The RHgene34 protein </span><span style="font-size:10.0pt / font-family:&quot / Arial&quot / ,&quot / sans-serif&quot / ">contains conserved motifs of esterases/lipases, such as HGGG (residues 95-98),GxSxG (residues 167 - 171) and the putative catalytic triad composed of Ser157,Asp255 and His285. The gene was cloned and expressed in pET21a(+), and transformed into <i>Escherichia coli </i>Rosetta. <i>p</i>-Nitrophenol (<i>p</i>-Np) fatty acyl esters of different carbon chain lengths were used for kinetic characterisation of RHgene34. </span><span style="font-size:10.0pt / font-family:&quot / Arial&quot / ,&quot / sans-serif&quot / ">Kinetic analysis revealed that RHgene34 had a broad range activity on the <i>p</i>-Npesters, from C2 - C14. RHgene34 operates optimally at 45 &ordm / C, pH 9.0 and has a half life of 30 mins at 45 &ordm / C. This study demonstrates that functional screening combined with the sequence analysis is a useful approach for isolating novel enzymes from ametagenome.</span></p> <p style="margin-bottom:0cm / margin-bottom:.0001pt / text-align: justify / line-height:normal / mso-layout-grid-align:none / text-autospace:none" class="MsoNormal"><span style="font-size:12.0pt / font-family:&quot / Arial&quot / ,&quot / sans-serif&quot / "><br type="_moz" /> </span></p> <br /> <p style="margin-bottom:0cm / margin-bottom:.0001pt / text-align: justify / line-height:normal / mso-layout-grid-align:none / text-autospace:none" class="MsoNormal"><span style="font-size:12.0pt / font-family:&quot / Arial&quot / ,&quot / sans-serif&quot / "><br type="_moz" /> </span></p> <br />

This dissertation describes the characterization of layer-by-layer silica and titania coatings deposited using a protamine-induced method. It was found that silica coatings were thinner and more porous than titania coatings. These coatings were functionalized by immobilizing modified Glucose oxidase during the layer-by-layer buildup. The enzyme was found to retain higher activity in silica versus titania, with full retention of activity observed in one configuration. Immobilization in both materials resulted in enhanced thermal stability and proteolytic protection. The enzyme-functionalized coatings were then modified by the immobilization of silver nanoparticles to the exterior, and this biological/inorganic composite was tested for its antimicrobial activity against E. coli and S. aureus. Against E. coli the composite worked in a synergistic fashion, showing more potent antimicrobial activity when compared to either agent used alone. The enzyme modification method was then extended to Laccase, which was immobilized to carbon nanotubes and characterized as a biocathode. Modified laccase returned a nearly two-fold higher current density versus the native enzyme. Finally, synthetic peptides were tested for their ability to adsorb to silica and titanium-oxide surfaces and subsequently deposit titanium-oxide coatings, in an effort to better understand the structure-function relationships of mineralizing peptides.

No description available.

The thesis presented here describes the steps that were taken in an attempt to solve the protein structure of MenD via molecular replacement and multiple wavelength anomalous dispersion. The introduction provides background on menaquinone biosynthesis and the role of MenD in this metabolic pathway. Also, a detailed discussion of the DC Family of enzymes, a subgroup of ThDP dependent enzymes, which MenD is a part of, is included.<p> Utilizing various software packages a 1.9 Å data set was processed and analyzed in an attempt to provide a molecular replacement result. When molecular replacement was deemed incapable of solving the phase problem of the data set, the production of SeMet protein was attempted to allow for MAD phasing.<p> A homology model of MenD was produced using the program Modeller with benzaldehyde lyase as a template. A structure based sequence alignment was done with all DC Family enzymes with structures published. Then a second structure based sequence alignment was done to compare the same set to the Modeller model. This was done to gain a deeper understanding of MenD and how it interacts with its cofactors ThDP and Mg2+. Furthermore, these results were used to implicate potential active site residues.

An enzyme-linked immunosorbent assay was developed to measure specific antibody response in bovine sera to bovine adenovirus type 3 (BA3), an etiologic agent of respiratory disease causing economic losses annualy to the cattle industry. Observed endpoint titers were determined using the intersection point from optical density values of serially diluted sera with a positive-negative threshold. Regression equations were determined from standards with titers ranging from low to high and used to predict ELISA titers from a single-serum dilution. A near-linear relationship existed between the observed and predicted ELISA titers of 118 bovine sera (r=0.9261). Predicted ELISA titers were determined using the single-dilution method for another 76 bovine sera and the correlation between the ELISA titers and serum-virus neutralization titers for these sera indicated a strong linear trend (r=0.8172). Both the ELISA and serum-virus neutralization titers on the bovine sera tested indicated widespread exposure to several types of bovine adenovirus. Although detection of active infection would still require examination of sera over time for evidence of a rising titer, the single-dilution ELISA devised should provide a rapid and sensitive method for detection of antibody response to bovine adenovirus type 3. / Graduation date: 1992

The Glyoxalase system is composed of two metalloenzymes, Glyoxalase I and Glyoxalase II, that catalyze the conversion of toxic, metabolically produced alpha-ketoaldehydes, such as methyglyoxal, in the presence of a thiol cofactor, such as glutathione, into their corresponding nontoxic 2-hydroxycarboxylic acids, leading to detoxification of these cellular metabolites. Previous studies on the first enzyme in the Glyoxalase system, Glyoxalase I (GlxI), in yeast, protozoa, animals, human, plants and Gram-negative bacteria suggest two metal activation classes, zinc-activation or non-zinc-activation (but exhibiting selective nickel/cobalt-activation). This thesis provides the key discoveries of the Glyoxalase system from Gram-positive microorganisms using the major thiol cofactor/cosubstrate that produced within that particular organisms as well as the relatedness of the proteins in the same beta-alpha-beta-beta-beta protein superfamily.

The thesis presented here describes the steps that were taken in an attempt to solve the protein structure of MenD via molecular replacement and multiple wavelength anomalous dispersion. The introduction provides background on menaquinone biosynthesis and the role of MenD in this metabolic pathway. Also, a detailed discussion of the DC Family of enzymes, a subgroup of ThDP dependent enzymes, which MenD is a part of, is included.<p> Utilizing various software packages a 1.9 Å data set was processed and analyzed in an attempt to provide a molecular replacement result. When molecular replacement was deemed incapable of solving the phase problem of the data set, the production of SeMet protein was attempted to allow for MAD phasing.<p> A homology model of MenD was produced using the program Modeller with benzaldehyde lyase as a template. A structure based sequence alignment was done with all DC Family enzymes with structures published. Then a second structure based sequence alignment was done to compare the same set to the Modeller model. This was done to gain a deeper understanding of MenD and how it interacts with its cofactors ThDP and Mg2+. Furthermore, these results were used to implicate potential active site residues.

Human T-cell lymphotropic virus type I (HTLV-I) is a retrovirus that is the causative agent of the fatal disease adult T-cell leukemia (ATL). HTLV-I silently infects over twenty million people worldwide; up to ten percent of these will develop ATL in their lifetime. There are currently no effective treatments for this disease. HTLV-I expresses its genome as polypeptides that must be processed in order to produce infectious virions. Like other retroviruses, HTLV-I encodes an aspartic acid protease to process these polypeptides into mature form. Because the protease is essential in the virus life cycle, it is an attractive target for the treatment of HTLV-I-induced ATL. The present work examines the structure and function of HTLV-I protease. A theoretical structure of the protease is presented, and the function of the C-terminal extension is considered. In order to determine which residues are involved in binding substrate, two experiments were performed: first, several residues were mutated to the corresponding residues in HIV-1 protease to determine whether HTLV-I protease can be made to process an HIV-1 protease substrate; second, an alanine scan was performed to knock out individual residues to assess their importance in binding substrate. This work builds knowledge of the structure and function of HTLV-I protease. By understanding which residues play a role in binding substrate and by developing a clearer picture of the structure of the protease, it will be possible to develop specific inhibitors for HTLV-I protease.

Abstract The use of antibiotics in aquaculture may cause development of antibiotic resistance among pathogens infecting cultured animals and humans. Therefore, the phages were isolated from the culture environment that can infect the pathogen and resistant bacteria. In this study, there were vibriophage and antibacterial phage isolated from CLOZ andSCKF. The small and circle plaque of vibriophage could become striking by decrease in top agar percentage. The electron micrographs of vibriophage and antibacterial phage belonged to the Podoviridae and Myroviridae family. The phages genome could be cut by HidinIII. The different size fragments were compared and matched to similar genome size of phages from NCBI. For the result, vibriophage may belong to the Picovirinae in Podoviridae. The antibacterial phage would be classified into either Mu-like viruses or unclassified Myoviridae. In the infecting test with (103 PFU/ml), the vibriophage lysing the host cell was not evident. Then, infecting with ϕA, ϕ20 and ϕ70 107 PFU/ml), the ϕA could lyse the cell and test the lowest OD after two hours by infecting. ϕ20 lysed the cell at exponential phase and antibacterial phage ϕ70 could lysed the host cell at different ages after six hours by infecting. A could lyse the cell and test the lowest OD after two hours by infecting. ϕ20 lysed the cell at exponential phase and antibacterial phage ϕ70 could lysed the host cell at different ages after six hours by infecting.

There are some 15,000 known organophosphorus chemicals. Some of these OP’s, including VX and paraoxon, demonstrate an acute neurotoxicity due to the inhibition of cholinergic enzymes. Organophosphorus chemical warfare agents and pesticide neurotoxins are subject to hydrolysis by OP degrading enzymes. To be useful as a bioremediation or anti-chemical warfare agent, the enzyme must be tailored for, and integrated into, a practical application platform. Several studies have established enzyme-based countermeasures, describing such diverse applications as decontaminating foams for surface remediation, encapsulating enzyme with liposome for in vivo therapy, enzyme attachments to surfaces for biosensors and development of a corn expression system for large-scale enzyme production. The goal of the research described here is to select, investigate and improve the operational potential of organophosphate-degrading enzymes including Organophosphorus Hydrolase (OPH, 3.1.8.1) and Organophosphorus Acid Anhydrolase (OPAA, 3.1.8.2). Using saturation kinetics, the catalytic efficiencies of these two major detoxification enzymes were characterized with substrates representing each class of OP neurotoxin, phosphotriester, phosphothioate and phosphofluoridate. OPH presents superior kinetic parameters with each OP class tested. Variants of OPH were created to increase the operational effectiveness of OP hydrolytic enzymes against phosphorothioates. An H254S/H257L mutation in the active site resulted in an improvement in the kinetics (kcat/KM) for the phosphorothioate, demeton-S. To screen potential vascular protection therapies, an in vitro protocol was developed to predict enzymatic effectiveness for protection of acetylcholinesterase from acute OP-inhibition. The protection abilities of the enzymes were directly related to their second order rate constants as inhibitory levels of OP are below the KM of the enzymes. Consideration of contaminant nature concentration and enzyme kinetic parameters, kcat and KM, is critical to understanding decontamination and effective use of enzyme technology. These technologies continue to develop and provide promising new decontamination tools for OP compounds.