Academic literature on the topic 'Yeast propagation'

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Journal articles on the topic "Yeast propagation"

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Tuite, Mick F., and Brian S. Cox. "Propagation of yeast prions." Nature Reviews Molecular Cell Biology 4, no. 11 (November 2003): 878–90. http://dx.doi.org/10.1038/nrm1247.

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Blanco, Carlos A., Julia Rayo, and José M. Giralda. "Improving Industrial Full-Scale Production of Baker's Yeast by Optimizing Aeration Control." Journal of AOAC INTERNATIONAL 91, no. 3 (May 1, 2008): 607–13. http://dx.doi.org/10.1093/jaoac/91.3.607.

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Abstract This work analyzes the control of optimum dissolved oxygen of an industrial fed-batch procedure in which baker's yeast (Saccharomyces cerevisiae) is grown under aerobic conditions. Sugar oxidative metabolism was controlled by monitoring aeration, molasses flows, and yeast concentration in the propagator along the later stage of the propagation, and keeping pH and temperature under controlled conditions. A large number of fed-batch growth experiments were performed in the tank for a period of 16 h, for each of the 3 manufactured commercial products. For optimization and control of cultivations, the growth and metabolite formation were quantified through measurement of specific growth and ethanol concentration. Data were adjusted to a model of multiple lineal regression, and correlations representing dissolved oxygen as a function of aeration, molasses, yeast concentration in the broth, temperature, and pH were obtained. The actual influence of each variable was consistent with the mathematical model, further justified by significant levels of each variable, and optimum aeration profile during the yeast propagation was found.
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Gibson, Brian R., Neil S. Graham, Chris A. Boulton, Wendy G. Box, Stephen J. Lawrence, Robert S. T. Linforth, Sean T. May, and Katherine A. Smart. "Differential Yeast Gene Transcription during Brewery Propagation." Journal of the American Society of Brewing Chemists 68, no. 1 (January 2010): 21–29. http://dx.doi.org/10.1094/asbcj-2009-1123-01.

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Crapeau, Myriam, Laurent Maillet, and Christophe Cullin. "Ploidy controls [URE3] prion propagation in yeast." FEMS Yeast Research 14, no. 2 (November 8, 2013): 324–36. http://dx.doi.org/10.1111/1567-1364.12110.

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Manzano, S., S. Vargas, G. Casaubon, and Á. González. "Evaluation of an active yeast propagation system on fermentation traits and quality of C.V. Carmenère wine." BIO Web of Conferences 12 (2019): 02009. http://dx.doi.org/10.1051/bioconf/20191202009.

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Active dry yeasts (ADY, Saccharomyces cerevisiae) are widely used in oenology due to their potential benefits on the control of fermentation and quality reproducibility among other aspects. On the other hand, yeast propagation systems, so called Active Yeast Systems (AYS), can be useful to optimize the alcoholic fermentation (AF) initial lag phase and reduce production costs. The objective of this work was to determine the predominance of an ADY strain propagated by AYS and the impact of this inoculum on cv. Carmenère wine quality. Lalvin ICV D21 ADY strain was inoculate according to the protocol recommended by the manufacturer (T0), and in parallel, it was propagate by the AYS and then used as inoculum (T1). Yeast strain predominance analyzed by restriction fragment length polymorphism (RFLP) technique indicates that nine (out of 9) yeast colonies obtained from a single sample of the ADY, show the same electrophoretic pattern when compared to the ADY. The results show limited significant differences for the fermentation speed and the yeast cell counting. The result of the physicochemical analysis of the musts and resulting wines showed no significant differences between treatments. A triangular test showed no significant sensory differences between wines
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Kurz, T., J. Mieleitner, T. Becker, and A. Delgado. "A Model Based Simulation of Brewing Yeast Propagation." Journal of the Institute of Brewing 108, no. 2 (2002): 248–55. http://dx.doi.org/10.1002/j.2050-0416.2002.tb00548.x.

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Malato, Laurent, Suzana Dos Reis, Laura Benkemoun, Raimon Sabaté, and Sven J. Saupe. "Role of Hsp104 in the Propagation and Inheritance of the [Het-s] Prion." Molecular Biology of the Cell 18, no. 12 (December 2007): 4803–12. http://dx.doi.org/10.1091/mbc.e07-07-0657.

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The chaperones of the ClpB/HSP100 family play a central role in thermotolerance in bacteria, plants, and fungi by ensuring solubilization of heat-induced protein aggregates. In addition in yeast, Hsp104 was found to be required for prion propagation. Herein, we analyze the role of Podospora anserina Hsp104 (PaHsp104) in the formation and propagation of the [Het-s] prion. We show that ΔPaHsp104 strains propagate [Het-s], making [Het-s] the first native fungal prion to be propagated in the absence of Hsp104. Nevertheless, we found that [Het-s]-propagon numbers, propagation rate, and spontaneous emergence are reduced in a ΔPaHsp104 background. In addition, inactivation of PaHsp104 leads to severe meiotic instability of [Het-s] and abolishes its meiotic drive activity. Finally, we show that ΔPaHSP104 strains are less susceptible than wild type to infection by exogenous recombinant HET-s(218–289) prion amyloids. Like [URE3] and [PIN+] in yeast but unlike [PSI+], [Het-s] is not cured by constitutive PaHsp104 overexpression. The observed effects of PaHsp104 inactivation are consistent with the described role of Hsp104 in prion aggregate shearing in yeast. However, Hsp104-dependency appears less stringent in P. anserina than in yeast; presumably because in Podospora prion propagation occurs in a syncitium.
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Crapeau, Myriam, Christelle Marchal, Christophe Cullin, and Laurent Maillet. "The Cellular Concentration of the Yeast Ure2p Prion Protein Affects Its Propagation as a Prion." Molecular Biology of the Cell 20, no. 8 (April 15, 2009): 2286–96. http://dx.doi.org/10.1091/mbc.e08-11-1097.

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The [URE3] yeast prion is a self-propagating inactive form of the Ure2p protein. We show here that Ure2p from the species Saccharomyces paradoxus (Ure2pSp) can be efficiently converted into a prion form and propagate [URE3] when expressed in Saccharomyces cerevisiae at physiological level. We found however that Ure2pSp overexpression prevents efficient prion propagation. We have compared the aggregation rate and propagon numbers of Ure2pSp and of S. cerevisiae Ure2p (Ure2pSc) in [URE3] cells both at different expression levels. Overexpression of both Ure2p orthologues accelerates formation of large aggregates but Ure2pSp aggregates faster than Ure2pSc. Although the yeast cells that contain these large Ure2p aggregates do not transmit [URE3] to daughter cells, the corresponding crude extract retains the ability to induce [URE3] in wild-type [ure3-0] cells. At low expression level, propagon numbers are higher with Ure2pSc than with Ure2pSp. Overexpression of Ure2p decreases the number of [URE3] propagons with Ure2pSc. Together, our results demonstrate that the concentration of a prion protein is a key factor for prion propagation. We propose a model to explain how prion protein overexpression can produce a detrimental effect on prion propagation and why Ure2pSp might be more sensitive to such effects than Ure2pSc.
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Nielsens, Olau. "Status of the yeast propagation process and some aspects of propagation for re-fermentation." Cerevisia 35, no. 3 (October 2010): 71–74. http://dx.doi.org/10.1016/j.cervis.2010.09.003.

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Guinan, Emma, and Gary Jones. "Influence of Hsp70 Chaperone Machinery on Yeast Prion Propagation." Protein & Peptide Letters 16, no. 6 (June 1, 2009): 582–86. http://dx.doi.org/10.2174/092986609788490168.

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Dissertations / Theses on the topic "Yeast propagation"

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Bradley, J. "Glucose biosensors for monitoring bakers yeast propagation." Thesis, Cranfield University, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.234492.

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Bariar, Bhawana. "Effects of the components of the Get pathway on prion propagation." Thesis, Atlanta, Ga. : Georgia Institute of Technology, 2007. http://hdl.handle.net/1853/26659.

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Thesis (M. S.)--Biology, Georgia Institute of Technology, 2008.
Committee Chair: Chernoff,Yury; Committee Member: Cairney,John; Committee Member: Choi,Jung; Committee Member: Doyle,Donald; Committee Member: Lobachev,Kirill. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Marchante, Ricardo Miguel Neto. "Analysis of propagation-defective mutations of the yeast (PSI+) prion." Thesis, University of Kent, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.587560.

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Analysis of how prions are propagated and transmitted in the yeast Saccharomyces cerevisiae has begun to reveal how an amyloid-forming protein can act as an epigenetic determinant of cell phenotype. Through the ability of prions to self propagate, genetic traits encoded by prions are inherently dominant, yet the underlying mechanism is only just beginning to emerge. One approach to elucidating the mechanism of prion propagation is to establish why certain mutations can impact negatively on inheritance of a prion-based trait. This thesis reports on a combined in vivo and structural analysis of one such class of mutant - PNM2-1 - a dominant negative mutation that inhibits propagation of [PS/+], the prion form of the translation termination factor Sup35p. The original PNM2-1 allele, a G58D mutation lies in one of a series of five oligopeptide repeats in the amino-terminal prion domain of the Sup35p (eRF3) and cells expressing this allele cannot efficiently propagate the [PS/+] prion. To establish the mechanism by which the PNM2-1 allele mediates this effect, a series of PNM2-1G58/G59/Y60 mutants of Sup35p was constructed. By combining genetic crossing, phenotypic analysis and solution NMR structural studies, a clear correlation between the conformational changes in the oligopeptide repeat caused by these mutations and the relative impact of these mutations on the in vivo propagation of [PS/+] was demonstrated. The conformational constraints associated with these mutations were also shown to the affect the ability of the protein to form and/or incorporate different of prion variants. These findings provide a molecular explanation of the dominant negative effects of PNM2-1 mutation on the maintenance of the [PS/+] prion and provide important new insights into the importance of conformation in prion propagation.
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Zizhou, Njodzi. "Studies on the fed-batch propagation of brewer's yeast in high gravity wort." Master's thesis, University of Cape Town, 2001. http://hdl.handle.net/11427/9751.

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The traditional batch brewing process is characterised by serial yeast propagation to build sufficient yeast for pitching. This results in cyclic variations in yeast environment, leading to a slow brewing process. In high gravity brewing the carbohydrate utilisation is inefficient as a result of the Crabtree effect that occurs in the presence of high sugar concentration. When optimising the brewing process the characteristics of conventional batch brewing should be maintained. Fed-batch propagation of yeast is used to improve carbohydrate utilisation and the yeast biomass formation by controlling nutrient supply.
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Moosavi, Behrooz. "The Role of Molecular Chaperone Hsp104 and its Co-chaperones in the Yeast [PSI+] Propagation." Thesis, University of Kent, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.499804.

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Wongwigkarn, Jintana. "Exploring the role of the molecular chaperone Hsp104 in yeast [PSI+] prion propagation and transmission." Thesis, University of Kent, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.633824.

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[PSI+] is the prion form of the Sup35 protein in Saccharomyces cerevisiae. The molecular Hsp 104 chaperone is involved in the propagation of the [PSI+] by dissolving Sup35p prion fibres into the small seeds (propagons) needed to generate a new round propagation. Overexpression of the HSP104 gene results in elimination of the [PSI+] prion, but the mechanism by which [PSI+] loss is triggered remains undetermined. To gain insight into the mechanism of such induced [PSr] elimination, the cellular factors with a known functional connection with Hsp104 and that may necessary for Hsp 104 overexpression-induced prion loss, were investigated. The Hsp90 cochaperones Cpr7p and Stilp that also bind to the C-terminus of Hspl04 are required for [PSI+] elimination by overexpression of both wild type Hsp104 and two different ATPase-defective mutants of Hspl04 but are not essential for [PSI+] prion propagation. This indicated that [PSr] elimination by elevated Hsp104 may occur as a consequence of activities of Hsp104 in addition to its remodelling activity.
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Tipton, Kimberly A. "Ordering the pathway of prion propagation in yeast through a structure/function analysis of Hsp104." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2008. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3297793.

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Jeřábková, Petra. "Studium vlastností biologického materiálu pomocí metod obrazové analýzy." Doctoral thesis, Vysoké učení technické v Brně. Fakulta chemická, 2010. http://www.nusl.cz/ntk/nusl-233311.

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Within the dissertation thesis “Study of Biological Material Attributes by Using Image Analysis Methods”, attention is focused on monitoring of the application of image analysis methods, mostly a fractal analysis, in studying the properties of various yeast species. The thesis includes determining the number of yeast cells and vegetative propagation of yeast using fractal parameters – fractal measure D and fractal dimension K. Attention is also paid not only to the application of the existing image analysis methods, but also to their renovation. The obtained images were evaluated using the box counting method specified by implementation of wavelet transformation. To monitor yeast cells for a longer time, it was first necessary to prepare a suitable microscopic preparation. To distinguish live and dead cells, the following fluorescent dyes were used: acridine orange, fluorescein diacetate, FUN-1, and Calcofluor White M2R. The images of yeast cells were recorded using a still camera or a CCD camera and microscope. Clips of the same size were obtained from the acquired digital photographs and processed by the HarFA program developed at the Faculty of Chemistry, Brno University of Technology. On the results it is possible to see a change in the fractal dimension depending on time, i.e. on the change of a budding cell structure, or to determine the number and radius of yeast cells upon predefined conditions.
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Tennant, Esther Paula. "Interactions of the chaperones and components of UB system in the formation and propagation of the yeast prion [PSI+]." Thesis, Available online, Georgia Institute of Technology, 2005, 2005. http://etd.gatech.edu/theses/available/etd-05292005-220155/.

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Crapeau, Myriam. "Facteurs cellulaires déterminant la propagation du prion [URE3] dans la levure Saccharomyces cerevisiae." Thesis, Bordeaux 2, 2010. http://www.theses.fr/2010BOR21728/document.

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Une protéine prion peut adopter deux conformations distinctes, l’une cellulaire et l’autre prion. La conformation prion est le résultat de son agrégation en fibre amyloïde. Cette fibre est le support de l’information prion à partir duquel les isoformes cellulaires sont convertis en forme prion de façon autocatalytique. La transmission de l’information prion repose donc sur la transmission de cette fibre au cours des divisions cellulaires, qui est réalisée par de petits polymères. Ceux-ci sont le résultat d’un équilibre entre la fragmentation et la polymérisation de la fibre. Une perturbation de cet équilibre provoque une agrégation massive de la protéine prion, menant à la perte de l’information prion.L’objectif de ma thèse était de comprendre ce qui définit in vivo la transmission du prion. Mon modèle d’étude est la protéine Ure2p propageant le prion [URE3] dans la levure S. cerevisiae. J’ai montré que la concentration cellulaire d’Ure2p détermine la vitesse d’agrégation de la protéine prion et donc son efficacité de transmission. En effet, de trop fortes concentrations cellulaires sont incompatibles avec la propagation du prion. La concentration cellulaire d’Ure2p définit également la diversité des souches prions. Un crible génétique m’a permit de mettre en évidence que la présence de séquences centromériques surnuméraires dans la cellule interfère avec la transmission du prion [URE3]. Le même phénomène est observé avec une augmentation du niveau de ploïdie de la cellule. Dans les deux cas, la surexpression du chaperon Hsp104 restaure une propagation normale du prion
A prion protein can adopt two distinct conformations, one cellular and one prion. Prion conformation is the result of its aggregation into amyloid fibers. This fiber is the support of the prion information from which the cellular isoforms are converted into prion form by autocatalytic manner. The prion information transmission is therefore based on the transmission of this fiber during cell division, which is done by small polymers. These are the result of a balance between fragmentation and polymerization of the fiber. A disturbance of this balance causes a massive aggregation of the prion protein, leading to the prion information loss.The objective of my thesis was to understand what defined in vivo the prion transmission. My studying model was the Ure2p protein propagating the [URE3] prion in S. cerevisiae yeast. I showed that the Ure2p cellular concentration determined the aggregation speed of the prion protein and thus its transmission efficiency. Indeed, too high cellular concentrations are incompatible with the prion propagation. The cellular concentration of Ure2p also defines the prion strains diversity. A genetic screen allowed me to highlight that the presence of centrometric supernumerary sequences in the cell interferes with the [URE3] prion transmission. The same phenomenon is observed with an increase in the cell ploidy. In both cases, overexpression of the Hsp104 chaperone restores normal prion propagation
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Book chapters on the topic "Yeast propagation"

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Hulse, G. A. "Yeast Propagation." In Brewing Yeast Fermentation Performance, 249–56. Oxford, UK: Blackwell Science, 2008. http://dx.doi.org/10.1002/9780470696040.ch23.

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Stewart, Graham G. "Yeast Culture Collections, Strain Maintenance and Propagation." In Brewing and Distilling Yeasts, 49–54. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-69126-8_4.

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Stear, Charles A. "Industrial Propagation and Production of Yeast for the Baking Industry." In Handbook of Breadmaking Technology, 469–78. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-2375-8_11.

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Masison, Daniel C. "Modulation of Amyloid Propagation in Yeast by Hsp70 and its Regulators and Chaperone Partners." In Protein Chaperones and Protection from Neurodegenerative Diseases, 277–314. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118063903.ch9.

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Quain, D. E. "Yeast supply and propagation in brewing." In Brewing, 167–82. Elsevier, 2006. http://dx.doi.org/10.1533/9781845691738.167.

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Quain, D. "Yeast supply and propagation in brewing." In Brewing. CRC Press, 2006. http://dx.doi.org/10.1201/9781439824603.ch8.

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Reidy, Michael. "The Role of the Hsp40 Chaperone Sis1 in Yeast Prion Propagation." In Prion - An Overview. InTech, 2017. http://dx.doi.org/10.5772/66449.

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Yang, Zi, Joo Hong, Irina Derkatch, and Susan Liebman. "Heterologous Gln/Asn-Rich Proteins Impede the Propagation of Yeast Prions by Altering Chaperone Availability." In Investigations in Yeast Functional Genomics and Molecular Biology, 165–206. Apple Academic Press, 2014. http://dx.doi.org/10.1201/b16586-10.

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"Heterologous Gln/Asn-Rich Proteins Impede the Propagation of Yeast Prions by Altering Chaperone Availability." In Investigations in Yeast Functional Genomics and Molecular Biology, 195–236. Apple Academic Press, 2014. http://dx.doi.org/10.1201/b16586-14.

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Rose, Alan B., and James R. Broach. "[22] Propagation and expression of cloned genes in yeast: 2-μm circle-based vectors." In Methods in Enzymology, 234–79. Elsevier, 1990. http://dx.doi.org/10.1016/0076-6879(90)85024-i.

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Conference papers on the topic "Yeast propagation"

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ROGOV, A. G., T. N. GOLEVA, K. K. EPREMYAN, I. I. KIREEV, and R. A. ZVYAGILSKAYA. "PROPAGATION OF PROOXIDANT-INDUCED OXIDATIVE STRESS WITHIN THE YEAST CELL." In HOMO SAPIENS LIBERATUS. TORUS PRESS, 2020. http://dx.doi.org/10.30826/homosapiens-2020-43.

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Reports on the topic "Yeast propagation"

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Harris, David A. Propagation of Mammalian Prions in Yeast. Fort Belvoir, VA: Defense Technical Information Center, July 2006. http://dx.doi.org/10.21236/ada472675.

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