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Yeast display

Ethanol Production from Cellulase-Displaying Yeast... [Pg.201]

Matano Y, Hasunuma T, Kondo A. (2013a). Cell recycle batch fermentation of high-solid lignocellulose using a recombinant cellulase-displaying yeast strain for high yield ethanol production in consolidated bioprocessing. Bioresour Technol, 135,403 09. [Pg.223]

Bacterial cell surface display Yeast cell surface display Mammalian cell surface display Ribosomal display Plasmid display... [Pg.221]

Figure 5.3 Direct conversion of starch to ethanol using (a) amylase-secreting or (b) amylase-displaying yeast cells. Figure 5.3 Direct conversion of starch to ethanol using (a) amylase-secreting or (b) amylase-displaying yeast cells.
For example, a screening of 416 strains (71 bacterial strains, 45 actinomycetes, 59 yeast, 60 basidiomycetes, 33 marine fungi, and 148 filamentous fungi) has been performed to look for microorganisms that display reductase activity in the absence of oxidase activity [8b]. A new microorganism, Diplogdasinospora grovesii IMI... [Pg.199]

Gai, S.A. and Wittrup, K.D. (2007) Yeast surface display for protein engineering and characterization. Current Opinion in Structural Biology, 17, 467 473. [Pg.78]

Chen, I., Choi, Y. A. and Ting, A. Y. (2007). Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins. J. Am. Chem. Soc. 129, 6619-25. [Pg.520]

Differences in post-translational modification (PTM) detail. Human therapeutic proteins produced in several recombinant systems (e.g. yeast-, plant- and insect-based systems Chapter 5) can display altered PTM detail, particularly in the context of glycosylation (Chapter 2). Some sugar residues/motifs characteristic of these systems can be highly immunogenic in humans. [Pg.78]

Attention has also focused upon a variety of additional production systems for recombinant biopharmaceuticals. Yeast cells (particularly Saccharomyces cerevisiae) display a number of characteristics that make them attractive in this regard. These characteristics include ... [Pg.110]

Most interferons have now been produced in a variety of expression systems, including E. coli, fungi, yeast and some mammalian cell lines, such as CHO cell lines and monkey kidney cell lines. Most interferons currently in medical use are recombinant human (rh) products produced in E. coli. E. coli s inability to carry out post-translational modifications is irrelevant in most instances, as the majority of human IFN-as, as well as IFN- 3, are not normally glycosylated. Whereas IFN-y is glycosylated, the E. coli-derived unglycosylated form displays a biological activity similiar to the native human protein. [Pg.225]

The glycosylated derivatives 51A-D were tested against the yeast Saccharomyces cerevisiae and displayed different photoactivities.24 In this case, the most photoactive compounds were the mono-glycosylated 51A and... [Pg.224]


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