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Expression of proteins in Pichia pastoris
2021The methylotrophic yeast Pichia pastoris is currently one of the most versatile and popular hosts for the production of heterologous proteins, including industrial enzymes. The popularity of P. pastoris stems from its ability to grow to high cell densities, producing high titers of secreted heterologous protein with very low amounts of endogenous ...
Giuliana, Mastropietro +2 more
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2019
The methylotrophic yeast Pichia pastoris (Komagataella phaffii) is used as an expression system for recombinant protein production for a variety of applications. It grows rapidly on inexpensive media containing methanol, glucose, glycerol, or ethanol as a sole carbon source. P.
Aysun, Türkanoğlu Özçelik +2 more
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The methylotrophic yeast Pichia pastoris (Komagataella phaffii) is used as an expression system for recombinant protein production for a variety of applications. It grows rapidly on inexpensive media containing methanol, glucose, glycerol, or ethanol as a sole carbon source. P.
Aysun, Türkanoğlu Özçelik +2 more
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Glycosylation in Pichia pastoris
Biotechnology and Applied Biochemistry, 1999The Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermentors. Another advantage of this system centres on the type of glycosylation that results, generally yielding protein ...
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Optimising Pichia pastoris Induction
2012A common method for inducing the production of recombinant proteins in Pichia pastoris is through the use of methanol. However, the by-products of methanol metabolism are toxic to yeast cells and therefore its addition to recombinant cultures must be controlled and monitored throughout the process in order to maximise recombinant protein yields ...
Zharain, Bawa, Richard A J, Darby
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Das Pichia pastoris-Expressionssystem
2012Die methylotrophe Hefe Pichia pastoris (P. pastoris, Abb. 15–1) wurde in den letzten Jahren weltweit erfolgreich als System zur heterologen Genexpression etabliert und gehort mittlerweile neben Escherichia coli (Kap. 14), Saccharomyces cerevisiae, Hansenula polymorpha, dem Baculovirus-Expressionssystem (Kap. 14), Saugerzellsystemen (Kap.
Reinhart, C., Krettler, C.
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Optimization of the Expression of Equistatin in Pichia pastoris
Protein Expression and Purification, 2002To improve the expression of equistatin, a proteinase inhibitor from the sea anemone Actinia equina, in the yeast Pichia pastoris, we prepared gene variants with yeast-preferred codon usage and lower repetitive AT and GC content. The full gene optimization approximately doubled the level of steady-state mRNA and protein accumulated in the culture ...
Outchkourov, N.S. +2 more
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Expression of Recombinant Proteins in Pichia Pastoris
Applied Biochemistry and Biotechnology, 2007Pichia pastoris has been used extensively and successfully to express recombinant proteins. In this review, we summarize the elements required for expressing heterologous proteins, and discuss various factors in applying this system for protein expression.
Pingzuo, Li +6 more
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Electroporation of Pichia pastoris
2014The introduction of foreign DNA into the yeast Pichia pastoris is similar to the processes used with Saccharomyces cerevisiae and routinely performed by the electroporation of plasmid DNA into electro-competent (E-comp) P. pastoris cells (Becker and Guarente, Methods Enzymol 194:182–187, 1991). Transformation of spheroplasts is more difficult (Cregg et
Knut Madden +2 more
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Engineering Pichia pastoris for the Production of Carotenoids
2018Carotenoids are one of the most diverse and widely distributed classes of pigments in the biosphere and exhibit a variety of functions in the nature. Their importance and biotechnological applications are higher and higher, but their sources are not increasing in the same exponential way.
Patricia, Veiga-Crespo +2 more
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Expression, Purification, and Characterization of Equistatin in Pichia pastoris
Protein Expression and Purification, 2000Equistatin (EI) is a cysteine protease inhibitor that was isolated from the sea anemone Actinia equina. It belongs to a recently discovered group of thyroglobulin type-I domain inhibitors called thyropins. Since native EI is found only in low amounts in the body of sea anemone and expression of recombinant EI in Escherichia coli yielded only 1 mg/liter
Rogelj, B. +3 more
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