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Дисертації з теми "Escherichia coli Inclusions"

Автор: Grafiati

Опубліковано: 4 червня 2021

Оновлено: 1 лютого 2022

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1

RODRIGUES, DANIELLA. "Utilização de altas pressões hidrostáticas para o estudo e renaturação de proteínas com estrutura quaternária." reponame:Repositório Institucional do IPEN, 2012. http://repositorio.ipen.br:8080/xmlui/handle/123456789/10161.

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Made available in DSpace on 2014-10-09T12:35:27Z (GMT). No. of bitstreams: 0<br>Made available in DSpace on 2014-10-09T14:06:25Z (GMT). No. of bitstreams: 0<br>Dissertação (Mestrado)<br>IPEN/D<br>Instituto de Pesquisas Energeticas e Nucleares - IPEN-CNEN/SP

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2

Wangsa-Wirawan, Norbertus Djajasantosa. "Physicochemical properties of protein inclusion bodies." Title page, contents and introduction only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phw2465.pdf.

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Bibliography: leaves 182-198. Improvements in the current production system of inclusion bodies and the downstream processing sequence are essential to maintain a competitive advantage in the market place. Optimisation of fermentation is considered to improve production yield; then flotation as a possible inclusion body recovery method.

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3

BALDUINO, KELI N. "Renaturacao em altas pressoes hidrostaticas de proteinas recombinantes agregadas em corpos de inclusao produzidos em Eschirichia coli." reponame:Repositório Institucional do IPEN, 2009. http://repositorio.ipen.br:8080/xmlui/handle/123456789/9457.

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Made available in DSpace on 2014-10-09T12:26:58Z (GMT). No. of bitstreams: 0<br>Made available in DSpace on 2014-10-09T14:03:47Z (GMT). No. of bitstreams: 0<br>Dissertacao (Mestrado)<br>IPEN/D<br>Instituto de Pesquisas Energeticas e Nucleares - IPEN-CNEN/SP

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4

Wong, Heng Ho. "Modelling studies of the interaction between homogenisation, centrifugation and inclusion body dissolution /." Title page, contents and summary only, 1997. http://web4.library.adelaide.edu.au/theses/09PH/09phw8718.pdf.

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5

Saulou, Claire. "Evaluation des propriétés anti-adhésives et biocides de films nanocomposites avec inclusions d’argent, déposés sur acier inoxydable par procédé plasma." Toulouse, INSA, 2009. http://eprint.insa-toulouse.fr/archive/00000315/.

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Dans le secteur biomédical et l’industrie agro-alimentaire, l’adhésion de microorganismes contaminants aux surfaces engendre de multiples impacts négatifs, à la fois en termes de santé publique, d’hygiène et de sécurité alimentaire. Dans ce contexte, l’objectif de l’étude est de mettre au point un traitement de surface de l’acier inoxydable 316L, afin de prévenir la colonisation microbienne. La modification des surfaces d’acier par traitement chimique ou physique n’a eu aucune incidence sur le détachement de Saccharomyces cerevisiae, évalué in vitro à l’aide d’une chambre à écoulement cisaillé

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6

Hart, Roger A. Bailey James E. Bailey James E. "Characterization of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli /." Diss., Pasadena, Calif. : California Institute of Technology, 1991. http://resolver.caltech.edu/CaltechETD:etd-06272007-152616.

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7

Olbrich, Richard. "The characterisation and recovery of protein inclusion bodies from recombinant Escherichia-coli." Thesis, University College London (University of London), 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324583.

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8

Garcia, i. Fruitós Elena. "Regulation of recombinant proteína solubility and conformational quality in Escherichia coli." Doctoral thesis, Universitat Autònoma de Barcelona, 2008. http://hdl.handle.net/10803/3923.

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All the processes that take place in a cell require one or more proteins, meaning that they are essential components of life. Proteins are macromolecules consisting of amino acid units, all of them being constructed with combinations of only 20 amino acids. The primary structure of a protein molecule is determined by the sequence of amino acids connected by peptide bonds forming a polypeptide chain. Once the amino acid chain is synthesized, the protein folds by a physical process that might be eventually assisted by other proteins, reaching its characteristic three‐dimensional structure

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9

Mikkola, Isak. "Does SCP-2 promote the expression of foreign proteins in Escherichia coli?" Thesis, Linköpings universitet, Biologi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-129802.

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Expression of foreign proteins in host organisms usually results in the development of insoluble, inactive proteins. Further, these proteins have a tendency to form aggregates termed inclusion bodies. However, the formation of inclusion bodies can be avoided by fusing the gene encoding the foreign protein to a highly soluble protein. In this report Sterol Carrier Protein-2 (SCP-2) is reviewed as a possible solubility tag. The experiment was carried out by fusing SCP-2 to one of two i nsoluble proteins, Green fluorescent protein (GFP) or a form of chloramphenicol acetyl transferase (CAT∆9). The

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10

Hedhammar, My. "Strategies for facilitated production of recombinant proteins in escherichia coli." Doctoral thesis, KTH, School of Biotechnology (BIO), 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-471.

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<p>The successful genomic era has resulted in a great demand for efficient production and purification of proteins. The main objective of the work described in this thesis was to develop methods to facilitate recovery of target proteins after recombinant production in Escherichia coli.</p><p>A positively charged purification tag, Z<sub>basic</sub>, has previously been constructed by protein design of a compact three-helix bundle domain, Z. The charged domain was investigated for general use as a fusion partner. All target proteins investigated could be selectively captured by ion-exchange chro

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11

Hoffmann, Daniel [Verfasser]. "Produktion des Insektenmetalloprotease Inhibitors in Escherichia coli : Neuartige Plattformtechnologie für die inclusion body-basierte Produktaufarbeitung / Daniel Hoffmann." Aachen : Shaker, 2019. http://d-nb.info/1190525623/34.

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12

Hedhammar, My. "Strategies for facilitated protein recovery after recombinant production in Escherichia coli." Doctoral thesis, KTH, Proteomik, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-471.

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Анотація:

The successful genomic era has resulted in a great demand for efficient production and purification of proteins. The main objective of the work described in this thesis was to develop methods to facilitate recovery of target proteins after recombinant production in Escherichia coli. A positively charged purification tag, Zbasic, has previously been constructed by protein design of a compact three-helix bundle domain, Z. The charged domain was investigated for general use as a fusion partner. All target proteins investigated could be selectively captured by ion-exchange chromatography under con

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13

Boström, Maria. "Design of substrate induced transcription for control of recombinant protein production in Escherichia coli." Doctoral thesis, KTH, Biotechnology, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3834.

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14

Henderson, Ian. "Solving the inclusion body problem - a case study : high level expression of TEM-1 #beta#-lactamase in Escherichia coli." Thesis, University of Warwick, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.282432.

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15

Truong, Vy Thuy. "Effect of cinnamic acid-cyclodextrin inclusion complexes on populations of Escherichia coli O157:H7 and Salmonella enterica in fruit juices." Thesis, Virginia Tech, 2007. http://hdl.handle.net/10919/35622.

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Cinnamic acid (CA) is a naturally occurring organic acid that is found in some fruits and a number of spices. CA has antimicrobial activity against certain spoilage microorganisms and pathogenic bacteria. However, the acid is poorly soluble in water. Cyclodextrin molecules have a hydrophobic cavity that allows them to serve as a host for insoluble molecules in aqueous matrices. This study was conducted to determine if the aqueous solubility of cinnamic acid could be improved via complexation with Î±- or Î²-cyclodextrins, and if these complexes could be used to control bacterial pathogens in

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16

Gomes, Fernanda Resende. "Expressão do fator estimulador de colônia de granulócito humano recombinante (rhG-CSF) em Escherichia coli." Universidade de São Paulo, 2010. http://www.teses.usp.br/teses/disponiveis/87/87131/tde-13082010-163827/.

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O Fator estimulador de colônias de granulócitos humano recombinante (rhG-CSF) produzido em Escherichia coli é uma proteína não glicosilada com 175 aminoácidos, de grande importância clínica para o tratamento de neutropenias. O presente trabalho propõe a construção de dois sistemas de expressão em E. coli, um sistema para obtenção do rhG-CSF no citoplasma e outro para secreção da proteína recombinante no meio de cultura utilizando a sequência sinal da L-asparaginase II. Os dois sistemas de expressão foram testados e comparados. A partir desses dados, passou-se para as etapas de obtenção do rhG-

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17

Le, Thanh Ha. "Optimisation of active recombinant protein production, exploring the impact of small heat-shock proteins of Escherichia coli, IbpA and IbpB, on in vivo reactivation of inclusion bodies." [S.l. : s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975691554.

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18

Reitz, Christian [Verfasser], Peter [Akademischer Betreuer] Neubauer, Peter [Gutachter] Neubauer, Vera [Gutachter] Meyer, and Ralf [Gutachter] Takors. "Impacts of oscillating cultivation conditions on the quality of recombinant inclusion bodies in Escherichia coli / Christian Reitz ; Gutachter: Peter Neubauer, Vera Meyer, Ralf Takors ; Betreuer: Peter Neubauer." Berlin : Technische Universität Berlin, 2017. http://d-nb.info/1156012856/34.

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19

Lu, Ping [Verfasser], Peter [Akademischer Betreuer] Neubauer, Peter [Gutachter] Neubauer, and Thomas [Gutachter] Schweder. "Response of Escherichia coli processes for the production of heterologous inclusion bodies by oscillating cultivation conditions in a scale-down bioreactor / Ping Lu ; Gutachter: Peter Neubauer, Thomas Schweder ; Betreuer: Peter Neubauer." Berlin : Technische Universität Berlin, 2016. http://d-nb.info/1156016312/34.

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20

Sundström, Heléne. "Analytical tools for monitoring and control of fermentation processes." Doctoral thesis, KTH, Skolan för bioteknologi (BIO), 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-4531.

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The overall objective of this work has been to adopt new developments and techniques in the area of measurement, modelling and control of fermentation processes. Flow cytometry and software sensors are techniques which were considered ready for application and the focus was set on developing tools for research aiming at understanding the relationship between measured variables and process quality parameters. In this study fed-batch cultivations have been performed with two different strains of Escherichia coli (E.coli) K12 W3110 with and without a gene for the recombinant protein promegapoieti

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21

Hart, Roger A. "Characterization of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli." Thesis, 1991. https://thesis.library.caltech.edu/2745/1/Hart_ra_1991.pdf.

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The process of inclusion body (IB) formation in the gram-negative bacterium Escherichia coli (E. coli) was investigated. The homodimeric hemeprotein Vitreoscilla hemoglobin (VHb) from the gram-negative bacterium Vitreoscilla was taken as the model protein. Expression of VHb under control of its native promoter from a pUC19-derived plasmid in strain JM101 lead to high-level accumulation of VHb in both soluble and insoluble forms. The soluble form was purified by sequential two-phase extraction techniques and used as a basis for analyzing the insoluble form. The amino acid content and N-termina

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22

Huang, Ji-Tzeng, and 黃繼增. "Refolding of the recombinant protein that forms inclusion bodies in Escherichia coli." Thesis, 2000. http://ndltd.ncl.edu.tw/handle/13919387326374696082.

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碩士<br>國立中興大學<br>農業生物科技學研究所<br>88<br>Abstract The Escherichia coli expression system is by far the best way for the over-expression of recombinant proteins. However, one of the major obstacles in utilizing E. coli for over-expressing recombinant proteins arises from inclusion body formation. The over-expressed recombinant proteins appear in an insoluble form. In order to make the recombinant proteins soluble, strong protein denaturant such as 8 M urea or 6 M guanidinium hydrochloride is used. Subsequently, urea or guanidinium hydrochloride is removed gradually by dialysis to allow re

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23

Huang, Shin-Wei, and 黃信維. "Minimize Periplasmic Inclusion Body Formation for Overproduction of Recombinant Penicillin Acylase in Escherichia coli." Thesis, 2001. http://ndltd.ncl.edu.tw/handle/25214746240080982345.

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碩士<br>逢甲大學<br>化學工程學系<br>89<br>To produce penicillin acylase (PAC) by recombinant DNA technology in Escherichia coli (E. coli), the overproduction was often limited by periplasmic processing and inclusion bodies were formed at a large amount in the periplasm. This raises an important issue that, for the overproduction of recombinant proteins, not only the transcriptional and/or translational efficiency has to be increased but also a ‘balanced’ protein synthesis flux throughout various gene expression (i.e., transcription, translation, and posttranslational processing) and folding steps should b

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24

CHENG, CHIH-YU, and 鄭志宇. "Purification of Recombinant AsChi61, a chitinase in Aeromonas schubertii from Inclusion Body of Escherichia coli." Thesis, 2017. http://ndltd.ncl.edu.tw/handle/v8rpf3.

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25

Li, Ruei-Yu, and 李瑞俞. "Study of Inclusion Body Formation under Various Culture Conditions in Recombinant Escherichia coli with Bioimaging System." Thesis, 2007. http://ndltd.ncl.edu.tw/handle/01602861630330623536.

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碩士<br>國立成功大學<br>化學工程學系碩博士班<br>95<br>The bioimaging system usually utilizes fluorescence protein as a reporter gene in eukaryotic systems, and it gives us an easy way to real-time monitor the distribution of fluorescence protein in cells. Eukaryote is thousand times the size of prokaryote, so it is not suitable to this system. In our research, giant protoplasts with size similar to Saccharomycete were prepared from recombinant Escherichia coli BL21(DE3)/pET-D7. The expression of D7 can be induced by IPTG to monitor inclusion body formation in real time. Using this approach, we can study inclusi

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26

JunXie, Yao, and 謝曜駿. "Study of Green Fluorescence Protein Inclusion Body Formation under Various Culture Conditions in Recombinant Escherichia coli with Bioimaging System." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/39510713938155070497.

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碩士<br>國立成功大學<br>化學工程學系碩博士班<br>98<br>Bioimaging system usually utilize fluorescence protein as a reporter gene in eukaryotic system, and it gives a easy way for us to real-time monitor the distribution of fluorescence protein in bacteria or cell.Eukaryote is thousand times the size of prokaryote, so it is not suitable to this system.In our reserach, recombinant Escherichia coli BL21(DE3)/ pET21a-GFP is used to prepare as giant protoplast which size is similar to saccharomycete with particular method. The expression of GFP can be induced by IPTG to real-time monitor inclusion body formation.Usin

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27

Narayanan, Niju. "Molecular and Genetic Strategies to Enhance Functional Expression of Recombinant Protein in Escherichia coli." Thesis, 2009. http://hdl.handle.net/10012/4721.

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The versatile Escherichia coli facilitates protein expression with relative simplicity, high cell density on inexpensive substrates, well known genetics, variety of expression vectors, mutant strains, co-overexpression technology, extracytoplasmic secretion systems, and recombinant protein fusion partners. Although, the protocol is rather simple for soluble proteins, heterologous protein expression is frequently encountered by major technical limitations including inefficient translation, formation of insoluble inclusion bodies, lack of posttranslational modification mechanisms, degradation by

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28

Vallejo, Gonzalez Luis Felipe. "Technical and kinetic aspects of the in vitro refolding process of bone morphogenetic protein-2 from Escherichia coli produced inclusion bodies /." 2006. http://www.gbv.de/dms/bs/toc/517553430.pdf.

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29

Le, Thanh Ha [Verfasser]. "Optimisation of active recombinant protein production, exploring the impact of small heat-shock proteins of Escherichia coli, IbpA and IbpB, on in vivo reactivation of inclusion bodies / by Than Ha Le." 2005. http://d-nb.info/975691554/34.

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30

Russell, Bonnie Leigh. "Expression, solubilisation, purification and characterisation of recombinant bluetongue virus viral protein 7." Diss., 2018. http://hdl.handle.net/10500/24951.

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Bluetongue virus belongs to the Orbivirus genus from the Reoviridae family. It infects predominantly domestic and wild ruminants and is economically significant worldwide. Bluetongue virus VP7 forms the intercepting layer between the outer capsid (VP2 and VP5) and VP3 which surrounds the genomic material. BL21(DE3), NiCo21(DE3), C43(DE3) pLysS and KRX Escherichia coli cells were transformed with a pET28a plasmid with the cDNA sequence encoding Bluetongue virus VP7. Expression of Bluetongue virus VP7 was tested at post induction temperatures between 16˚C and 37 ˚C, at inducer concentrations bet

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