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Purification of 1-aminocyclopropane-1-carboxylic acid N-malonyltransferase from mung bean hypocotylsTan, Qian, 譚茜 January 2008 (has links)
published_or_final_version / Biological Sciences / Master / Master of Philosophy
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"PyrH and PrnB crystal structures" /De Laurentis, Walter. January 2006 (has links)
Thesis (Ph.D.) - University of St Andrews, November 2006.
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Molybdenum hydroxylases from bovine kidney and liverBaum, Kenneth Michael. January 1900 (has links)
Thesis (M.S.)--The University of North Carolina at Greensboro, 2008. / Directed by Bruce Banks; submitted to the Dept. of Chemistry. Title from PDF t.p. (viewed Jul. 31, 2009). Includes bibliographical references (p. 95-102).
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Development of a novel dehydrogenase and a stable cofactor regeneration systemVázquez-Figueroa, Eduardo. January 2008 (has links)
Thesis (Ph.D)--Chemical Engineering, Georgia Institute of Technology, 2009. / Committee Chair: Bommarius, Andreas S.; Committee Member: Doyle, Donald F.; Committee Member: Koros, William J.; Committee Member: Moore, Jeffre C.; Committee Member: Prausnitz, Mark R. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Design, assessment, and future implications of the Multiple Enzyme Analyzer (MEA), a tool for in-situ monitoring of marine microbial activity /Jaeger, Stephanie A. January 1900 (has links)
Thesis (M.S.)--Oregon State University, 2007. / Printout. Includes bibliographical references. Also available on the World Wide Web.
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Structural studies of enzymes involved in propylene and acetone metabolism in Xanthobacter autotrophicusKrishnakumar, Arathi Mandyam. January 2007 (has links) (PDF)
Thesis (Ph.D.)--Montana State University--Bozeman, 2007. / Typescript. Chairperson, Graduate Committee: John W. Peters. Includes bibliographical references (leaves 155-169).
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Isolation and characterization of a novel thermostable and catalytically efficient laccase from Peniophora sp. strain UD4Jordaan, Justin January 2005 (has links)
Enzymes are becoming an effective tool in industrial processes, from crude applications such as bioremediation to fine processes such as chirally selective biocatalysis. The ligninolytic enzymes have recently received considerable attention for industrial application due to both their broad substrate range and their ability to degrade the most recalcitrant natural polymer, lignin. This group of enzymes was therefore identified as the target group for this study. Improved enzyme properties are constantly being sought to enhance the range of applications for enzymes. Biodiversity provides a wide variety of enzymes. Several researchers have concentrated on extremophiles as their primary source of superior enzymes, consequently neglecting temperate environments in their search for these enzymes. The relatively neglected fungal biodiversity of South Africa provided an opportunity to test the hypothesis that potentially important industrial enzymes with unusual properties could be isolated from mesophilic basidiomycetous fungi. Subsequent screening of Eastern Cape biodiversity for thermostable ligninolytic enzymes from basidiomycetes resulted in the isolation of a novel laccase enzyme from a basidiomycetous species. This fungus was identified as Peniophora sp. UD4 by phylogenetic analysis of rDNA ITS sequences. Initial studies indicated a superior optimum temperature of 70°C and thermostability, indicated by no loss in activity at 60°C over nine hours. Further characterization of the laccase revealed a broader than usual substrate range through its unusual ability to oxidatively couple DMAB and MBTH. The laccase also exhibited a broad pH oxidation range for ABTS (pH 2 – 6.8), and a relatively high affinity (K_m_ = 0.0123 mM) and catalytic efficiency (63 252 mM^(-1)^s^(-1)^) for ABTS as a substrate. The laccase activity from Peniophora sp. UD4 was shown to be comprised of three isozymes with a molecular weight of 62 kDa and pI’s of 6.33, 6.45 and 6.50. Investigation of the nutrient and physical factors affecting ligninolytic enzyme production and growth of Peniophora sp. UD4 indicated that the wild-type organism was unsuitable for large scale production of the thermostable laccase due to the low levels of laccase production. The thermostable laccase was applied to defouling of ultrafiltration membranes, bioremediation of industrial waste streams, biocatalysis, and biosensor technology as potential applications. Application of the Peniophora sp. UD4 laccase to defouling of membranes used for ultrafiltration of brown water showed large flux recoveries of 31, 21 and 21% after the first three defouling recycles respectively, compared to 3% for the control without immobilized enzyme. The novel laccase showed potential for the bioremediation of industrial waste streams, the most successful being that of bleach plant effluent, where a reduction of 66% of the phenolic load was achieved. Application of the novel laccase to biocatalytic oxidation of ferulic acid and (±)-α-pinene showed higher product yield as compared to oxidation of these compounds by Trametes versicolor laccase in mediated and non-mediated systems. The major products of (±)-α-pinene oxidation were identified as verbenol and trans-sorberol. The Peniophora sp. UD4 laccase was successfully applied to biosensor technology, which benchmarked significantly better than Trametes versicolor laccase for the detection of 4-chlorophenol. The biosensor developed with laccase from UD4 by covalent binding to a glassy carbon electrode exhibited the best combination of sensitivity and stability. This thesis shows that a laccase with superior properties was obtained from a mesophilic South African basidiomycete. The catalytic properties displayed by the novel laccase from Peniophora sp. UD4 all contribute to the increased industrial applicability of laccases, and may be the most industrially feasible enzyme of its class isolated to date.
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QueF and QueF-like: Diverse Chemistries in a Common FoldBon Ramos, Adriana 10 August 2016 (has links)
The tunneling fold (T-Fold) superfamily is a small superfamily of enzymes found in organisms encompassing all kingdoms of life. Seven members have been identified thus far. Despite sharing a common three-dimensional structure these enzymes perform very diverse chemistries.
QueF is a bacterial NADPH-dependent oxidoreductase that catalyzes the reduction of the nitrile group of 7-cyano-7-deazaguanine (preQ0) to a primary amine (preQ1) in the queuosine biosynthetic pathway. Previous work on this enzyme has revealed the mechanism of reaction but the cofactor binding residues remain unknown. The experiments discussed herein aim to elucidate the role of residues lysine 80, lysine 83, and arginine 125 (B. subtilis numbering) in NADPH binding. The biological role of the disulfide bond between the conserved residues cysteine 55 and cysteine 99 observed in several crystal structures is also examined.
Characterization of QueF mutants K80A, K83, R125A and R125K revealed lysine 80, lysine 83 and arginine 125 are required for turnover. Further analysis of turnover rates for R125K are consistent with this residue and both lysines being involved in cofactor binding presumably by interacting with the negatively charged phosphate tail of NADPH and are therefore involved in cofactor binding. Based on bond angles and energies, the disulfide bond between Cys55 and Cys99 was characterized as non-structural. Enzyme oxidation assays were consistent with the bond serving to protect QueF against irreversible oxidation of Cys55, which would render the enzyme inactive. This is the only known example of a stress protective mechanism in the Tunneling-fold superfamily.
QueF-like is an amidinotransferase found in some species of Crenarchaeota and involved in the biosynthesis of archaeosine-tRNA. The work presented here is focused on the preliminary characterization of this enzyme, including the elucidation of the natural substrate as well as the source of ammonia. The structure of the enzyme was solved and is also discussed.
Substrate analysis for QueF-like indicated this enzyme is capable of binding both preQ0 and preQ0-tRNA and reacting to form a thioimide intermediate analogous to QueF but only the latter serves as a substrate for the reaction. This makes QueF-like the first example of a nucleic acid binding enzyme in the Tunneling-fold superfamily. Ammonia, glutamine and asparagine were tested as nitrogen sources and unlike most known amidotransferases, QueF-like can only use free ammonia to produce the archaeosine-tRNA product. The crystal structure of P. calidifontis QueF-like indicates the functional enzyme is a dimer of pentamers pinned together by a large number of salt bridges. The structure presents a high degree of similarity to that of QueF albeit the higher twist of the QueF-like pentamers with respect to QueF results in a more compact structure.
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Degradation of sawdust by Cellulomonas fimi enzymesVondette, Nancy Anne January 1982 (has links)
Cellulomonas find was grown on minimal media with casamino acids and yeast extract added. Avicel was found to be the best cellulosic carbon source for the production of cellulase enzymes.
The Millipore Ultrafiltration System was found to be the most efficient method of concentrating the enzyme preparations.
Unpretreated sawdust samples of four different softwood species were degraded between 12 and 16 percent over a 15-day treatment. Increasing the concentration of substrate lead to a lower percent degradation but a higher overall degradation. Chemical pretreatment did not appreciably increase degradability of the samples. Physical pretreatments decrease the degrada-bility of the sawdust samples.
The lotech pretreatment, which is a combination of chemical and physical pretreatment, gives a substrate that is degraded by the Cellulomonas fimi enzyme preparation. The pretreatment makes 50% of the sample water soluble. In 3 days, a further 35% is degraded from large insoluble chunks into insoluble small particles which remain in suspension. There is 6% degraded into soluble state. This leaves only 9% of the initial sample left in the pellet. With longer incubation, one would expect the degradation to continue. / Science, Faculty of / Microbiology and Immunology, Department of / Graduate
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Enzyme modified magnetic nanoparticles : an approach for biomass conversion processes /Lucena, Guilherme Nunes. January 2020 (has links)
Orientador: Rodrigo Fernando Costa Marques / Resumo: A biomassa lignocelulósica vem se destacando como uma matéria-prima essencial para a produção de muitos produtos químicos de interesse industrial em áreas como a produção de energia, alimentos, fármacos, agricultura, meio ambiente e assim por diante. Apesar disso, muitas aplicações vêm esbarrando em uma série de dificuldades encontradas nos processos de conversão enzimática, como instabilidade operação das enzimas, alto custo de produção e purificação, reações de inibição e problemas de recuperação e reciclo. Para contornar esses problemas, muitos métodos de imobilização enzimática têm surgido, entre os quais, destaca-se a obtenção de agregados enzimáticos reticulados magnéticos (MCLEAs). Esta classe de materiais é obtida a partir da reação de reticulação entre agregados físicos de enzimas e suportes magnéticos, o qual pode unir as importantes propriedades catalíticas dos agregados físicos (como resultado da manutenção da estrutura nativa da enzima) à capacidade de recuperação e reciclo do suporte magnético (devido suas propriedades magnéticas intrínsecas). Frente a isso, esse trabalho relata a síntese, caracterização e potencial aplicação de MCLEAs de enzimas celulases em processos de conversão de celulose. Dividido em três capítulos, primeiramente é apresentado um review sobre o estado da arte no que diz respeito a obtenção de produtos de valor agregado a partir da biomassa lignocelulósica utilizando MCLEAs. No segundo capítulo, diferentes MCLEAs foram preparados na presenç... (Resumo completo, clicar acesso eletrônico abaixo) / Abstract: Lignocellulosic biomass has highlighted as an essential renewable raw material for production of many value-added chemicals of industrial interest in field as energy production, food, pharmaceutical, agriculture, environment and so on. Despite it, many applications have wrought with a series of difficulties in regarding enzymatic conversion processes, as enzyme operational instability, high production and purification cost, inhibition reactions, and issues of recovery and recycle. To overcome these issues, many enzyme immobilization methods have emerged, among which highlights the obtention of magnetic-cross linked enzyme aggregates (MCLEAs). This materials class is obtained from cross-linking reaction between enzyme physical aggregates and magnetic supports, which can gather the important catalytic properties of the physical aggregates (as a result of enzyme native structure maintenance) to recovery and recycle capacity of magnetic nanoparticles (as result of its intrinsic magnetic properties). Faced it, this work reports the synthesis, characterization and potential application of different cellulases MCLEAs in the cellulose enzymatic conversion process. Sectioned in three chapters, firstly is presented a review about the state of art in concern to obtention of value-added chemicals from lignocellulosic biomass using MCLEAs. In the second chapter, different MCLEAs were prepared in the presence of quitosana-coated magnetic nanoparticles with three different precipitation age... (Complete abstract click electronic access below) / Doutor
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