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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.

Die Expression humaner Proteine in der Hefe Pichia pastoris: Hochdurchsatzverfahren und bioinformatische Identifizierung von Expression-beeinflussenden Sequenzmerkmalen

Böttner, Mewes. January 2004 (has links) (PDF)
Berlin, Techn. Univ., Diss., 2004. / Computerdatei im Fernzugriff.

Funktionelle Expression von Channelrhodopsin 2 (ChR2) in der methylotrophen Hefe Pichia pastoris und biophysikalische Charakterisierung

Kirsch, Taryn. Unknown Date (has links) (PDF)
Frankfurt (Main), Universiẗat, Diss., 2008. / Erscheinungsjahr an der Haupttitelstelle: 2007.

Development and application of process analytical technology for fed-batch bioprocesses of the yeast Pichia pastoris

Ramireddy, Sreenivasula Reddy. January 1900 (has links)
Thesis (Ph.D.)--University of Nebraska-Lincoln, 2007. / Title from title screen (site viewed Mar. 27, 2008). PDF text: xxiii, 235 p. : ill. (some col.) ; 3 Mb. UMI publication number: AAT 3284719. Includes bibliographical references. Also available in microfilm and microfiche formats.

Etablierung von neuen Methoden zur Herstellung rekombinanter Antikörper und zur spezifischen Selektion von Antikörpervarianten im hohen Durchsatz

Lange, Stefan. January 2002 (has links)
Stuttgart, Univ., Diss., 2002.

Expression of CFTR and its transmembrane domains in E.coli and yeast

Gokce, Isa January 1999 (has links)
No description available.

Mechanismen der Elektropermeabilisierung und Elektrofusion eukaryotischer Zellen und Protoplasten

Endter, Jörg-Michael January 2008 (has links)
Würzburg, Univ., Diss., 2008. / Zsfassung in engl. Sprache.

Étude d'assemblage du virus de l'hépatite C : rôles de la "signal peptide peptidase" dans ce processus /

Gagné, Valérie. January 2004 (has links)
Thèse (M.Sc.)--Université Laval, 2004. / Bibliogr.: f. 78-88. Publié aussi en version électronique.

A novel spray-drying process to stabilize glycolate oxidase and catalase in Pichia pastoris and optimization of pyruvate production from lactate using the spray-dried biocatalyst

Glenn, James Huston. Subramanian, Mani. January 2009 (has links)
Thesis supervisor: Mani Subramanian. Includes bibliographic references (p. 121-125).

Cloning and expression of xylanase variants in Pichia pastoris

Govindarajulu, Natasha January 2017 (has links)
Submitted in fulfillment for the requirement of a Degree of Master in Biotechnology, Durban University of Technology, 2017. / Microbial xylanases have attracted considerable research interest because of their various applications in biotechnology including the biobleaching of kraft pulp, to increase the nutritional value of foods and animal feed as well as for their potential use in the production of ethanol and methane. In the paper and pulp industry, the bleaching process involves the use of toxic chemicals and in the interim produces harmful gases that have a negative impact on the environment. The application of enzymes for this process will potentially reduce the environmental pollution by this industry. In addition, using an enzyme that is thermostable and alkali tolerant means that they will remain active under the required processing conditions. The xylanase gene, xynA derived from Thermomyces lanuginosus DSM 5826, was previously evolved to produce a number of xylanase variants, which were further enhanced for increased thermostability and alkalinity. In this study, these variants were cloned in Pichia pastoris using the pBGP1 vector to achieve extracellular production of the recombinant proteins. The xylanase genes were isolated using PCR. Both vector and DNA inserts were linearized with restriction enzymes EcoRI and XbaI and ligated. Electroporation was employed to transform the yeast with the recombinant plasmids. This was followed by the expression of the enzymes in P. pastoris grown in yeast peptone glucose (YPD) medium. Enzyme activity was thereafter assessed and the yeast was found to produce 164, 78, 96 and 142 IU/ml of S325, S340, G41 and G53 xylanase respectively, higher levels than bacterial hosts. The enzymes were then characterized and it was established that the optimum temperatures and pH for maximum xylanase activity were, 60°C, pH 6 for S325; 40°C, pH 5 for S340; 60°C, pH 6 for G41 and 60°C, pH 7 for G53. i The pH and temperature stabilities of the respective enzymes were investigated, the S325 variant was exceptionally stable at a pH between 5 and 7 and temperature range of 40-80°C and retained a minimum of 40% of activity at higher pH and temperature after an incubation period of 90 min. The S340 variant was the least thermostable and alkali stable from all four variants, it however retained 40% of activity when subjected to conditions of pH 9, 80°C after 90 min. The G41 and G53 were highly stable under the pH and temperature conditions that they were subjected to. Thus being suitable for potential application in the pulp and paper industry. The enzymes were able to retain 80% of activity at pH 9, 80°C after 120 min. P. pastoris has been proven to be a more suitable protein expression vector than E. coli for a number of reasons, including; the ability to perform complex post-translational modifications and grow to high densities in minimal media resulting in the production of a high yield of heterologous proteins. / M

Characterization of Arabidopsis Glycoside Hydrolases Family 9 Genes

Li, Ya-ru 26 January 2010 (has links)
Generation of alcohol for biofuels from fermentation of sugar or starch has several economic disadvantages such as high cost of sugar processing and land usage competing with staple food. The solution may reside in hydrolysis of cellulose from crop waste such as stalks of rice and corn or non-crop plants such as weeds or wood. Our goal is to identify cellulases that can degrade cellulosic biomass more efficiently. Studies of microbial Family 9 glycoside hydrolase (GH9) proteins, including both endo-glucanases (EC and cellobiohydrolases (EC, have shown that they function through an inverting mechanism to cleave the 1, 4-£]-glucosidic bond between two unsubstituted Glc units. The main function of plant glycoside hydrolases are involved in polysaccharide metabolism of cell wall during cell growth. Twelve Arabidopsis thaliana (Columbia) endo-1,4-£]-glucanases that belong to the GH9, were cloned and expressed in Pichia pastoris in order to produce cellulases to facilitate efficient bio-alcohol production. The recombinant proteins do not show in vitro endo-1, 4-£]-glucanase activity, but we can detect the recombinant proteins expression in supernatant or in pellet. The lack of enzymatic activity from recombinant proteins is probably due to improper folding or glycosylation, or fast degradation resulted from the above reasons. Other bioreactor will be tested in the future. Genetic engineering to modify Arabidopsis thaliana (Columbia) endo-£]-1, 4-glucanases is another approach to produce functional cellulases with economic efficiency that can be adapted to industrial scale for alcohol generation. On the other hand, we use semi-quantitative PCR method to study the Arabidopsis GH9 genes expression level in different tissue. At4g39000 and At3g43860 were found only in flowers and inflorescence, and At1g65610 expression in roots and shoots of the amount of more. Other genes in different tissues, was no found significant difference.

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