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Saccharomyces S. cerevisiae

The overall life cycle of a particular yeast Saccharomyces (S.) cerevisiae, is summarised in Fig. S.6 which shows how it is possible for the cells to fuse to form various cell and spore types. The figure shows the possible types of reproduction in yeast. Generally, industrial strains of S. cerevisiae, brewers yeast, reproduce by budding/ fission processes and only sporulate under specialised conditions. However, many strains of yeast are capable of cell fusion to form spores or cells with increased genetic complements. Such strains have many sets of chromosomes and are termed polyploid. Active fermentation of industrial strains involves growth by mitotic division and nutrient depletion which results in stationary cells with little or no spore formation. [Pg.266]

Yeasts Saccharomyces S. cerevisiae (S. boulardii), S. pastorianus (S. carlsbergensis)... [Pg.146]

Saccharomyces cerevisiae S. cerevisiae var. ellipsoideus S. carlsbergensis S.fragilis S. rouxii S. delbrueckii... [Pg.285]

Saccharomyces yeasts are rapid fermentors. S. cerevisiae and S. bayanus produce up to 18—20% ethanol. The cells are ovoid to spherical, eUiptical, or elongated (especially under conditions of nitrogen starvation). Vegetative propagation is by multilateral budding. S. uvarum and S. rosei occur earher in the fermentation, when S. rosei may produce up to 6—8% ethanol before being overgrown by the other Saccharomyces yeasts. S. cerevisiae may produce up to 18-20% ethanol (28). [Pg.392]

It should be possible to extend the DNA microarray-binding experiment to whole-genome analysis of transcription factor binding sites. The authors suggest that a microarray spotted with 12,000 one-kilobase sequences would span the entire Saccharomyces cerevisiae genome (Bulyk et al., 2001). Such an array could be used to characterize the sequence specificity of S. cerevisiae transcription factors. These experiments would be useful for predicting functions of previously uncharacterized transcription... [Pg.100]

One of the first reports on yeast-mediated color removal by a putative process of biosorption of azo dyes by yeast (Rhodotorula sp.) biomass belongs to [31]. Yeast species such as Kluveromyces marxianus removed the diazo dye remazol black B [10], Candida catenulata and Candida kefyr removed more than 90% of amaranth by biosorption [6]. Biosorption uptake of the textile azo dyes remazol blue, reactive black, and reactive red by S. cerevisiae and C. tropicalis varied according to the selected dye, dye concentration, and exposure time [5, 7]. In a recent screening work carried out by [32], from the 44 yeast strains tested for their decolorization ability, 12 of them removed the dye Reactive Brilliant Red K-2BP by biosorption, among them the following were identified S. cerevisiae, Saccharomyces uvarum, Torulopsis Candida, and Saccharomycopsis lipolytica. [Pg.186]

Yeast expression vectors have been among those most commonly used since the beginning of gene technology. Vectors based on baker s yeast, Saccharomyces cerevisiae, have been especially popular for robust expression of many types of recombinant proteins [90]. For instance, the first commercially available recombinant vaccine, the hepatitis B surface antigen vaccine, was produced from an S. cerevisiae vector [91]. Many other recombinant proteins have also been efficiently expressed in yeast including al-Antitrypsin [92], insulin [93], Epstein-Barr virus envelope protein [94], superoxide dismutase [95] and interferon-a [90]. [Pg.22]

Molecular targets have been elucidated for Dm-AMPl and Rs-AFP2. Dm-AMPl was found to bind plasma membranes from Neurospora crassa and Saccharomyces cerevisiae in a saturable manner and it competed with closely related defensins for binding. Mutational studies with S. cerevisiae identified lipid raffs containing sphingolipids as a molecular target " while glycosylphosphatidylinositol (GPI)-anchored proteins could be... [Pg.263]

Figure 2.1 Structures of histone acetyltransferases (HATs). Ribbon representation of the structures of the HAT domains of (a) Tetrahymena thermophila CcnS (PDBcode Iqsr), (b) Saccharomyces cerevisiae Hatl (PDB code Ibob), (c) S. cerevisiae Esal (PDB code Imja),... Figure 2.1 Structures of histone acetyltransferases (HATs). Ribbon representation of the structures of the HAT domains of (a) Tetrahymena thermophila CcnS (PDBcode Iqsr), (b) Saccharomyces cerevisiae Hatl (PDB code Ibob), (c) S. cerevisiae Esal (PDB code Imja),...
There are two yeast expression hosts that have an established track record for high-level production of heterologous proteins, namely Saccharomyces cerevisiae and Pichia pastoris. HTP expression screening using microplate formats has been reported for both these yeasts by Lang and coworkers (Holz et ah, 2002, 2003 Boettner et ah, 2002). In both cases standard protocols have been miniaturized with cells cultured in either 1.5 ml cultures in 96-deep-well plates for S. cerevisiae or 2 ml cultures in 24-deep-well plates for P. pastoris. Soluble... [Pg.32]


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See also in sourсe #XX -- [ Pg.258 , Pg.418 ]




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