Topic
Pichia pastoris
About: Pichia pastoris is a research topic. Over the lifetime, 7937 publications have been published within this topic receiving 162645 citations. The topic is also known as: Komagataella pastoris.
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TL;DR: A WiKi based platform allows all users to create additional information on genes, proteins, physiology and other items of P. pastoris research, so that the Pichia community can benefit from exchange of knowledge, data and materials.
Abstract: The first genome sequences of the important yeast protein production host Pichia pastoris have been released into the public domain this spring. In order to provide the scientific community easy and versatile access to the sequence, two web-sites have been installed as a resource for genomic sequence, gene and protein information for P. pastoris: A GBrowse based genome browser was set up at http://www.pichiagenome.org and a genome portal with gene annotation and browsing functionality at http://bioinformatics.psb.ugent.be/webtools/bogas. Both websites are offering information on gene annotation and function, regulation and structure.
63 citations
TL;DR: Pichia pastoris may not serve as an adequate host for the site‐directed mutagenesis of T. reesei CBH I, and the yeast‐expressed enzyme showed non‐wild‐type secondary structure by circular dichroism.
Abstract: Pichia pastoris was transformed with the Trichoderma reesei cbh1 gene, and the recombinant enzyme was purified and analyzed kinetically and by circular dichroism The P pastoris rCBH I was recognized by MoAb raised to T reesei CBH I but was found in multiple molecular weight species on SDS-PAGE gels Carbohydrate content determination and SDS-PAGE western analysis indicated that the recombinant protein was hyperglycosylated, although a species very similar in molecular weight to the T reesei enzyme could be isolated chromatographically The P pastoris rCBH I also demonstrated activity toward soluble and insoluble substrates (ie, pNPL and Sigmacell), although at a level significantly lower than the wild-type enzyme More seriously, the yeast-expressed enzyme showed non-wild-type secondary structure by circular dichroism We conclude that P pastoris may not serve as an adequate host for the site-directed mutagenesis of T reesei CBH I
63 citations
TL;DR: The two most widely used species of yeast, Saccharomyces cerevisiae and Pichia pastoris, are compared and contrasted here.
Abstract: Having decided on yeast as a production host, the choice of species is often the first question any researcher new to the field will ask. With over 500 known species of yeast to date, this could pose a significant challenge. However, in reality, only very few species of yeast have been employed as host organisms for the production of recombinant proteins. The two most widely used, Saccharomyces cerevisiae and Pichia pastoris, are compared and contrasted here.
63 citations
TL;DR: The production of homogeneous glycoprotein species of recombinant horseradish peroxidase by using a P. pastoris platform strain in which OCH1 was deleted, which showed a growth impaired phenotype and considerable rearrangements of cell wall components, but nevertheless secreted more homogeneously glycosylated protein.
Abstract: The yeast Pichia pastoris is a common host for the recombinant production of biopharmaceuticals, capable of performing posttranslational modifications like glycosylation of secreted proteins. However, the activity of the OCH1 encoded α-1,6-mannosyltransferase triggers hypermannosylation of secreted proteins at great heterogeneity, considerably hampering downstream processing and reproducibility. Horseradish peroxidases are versatile enzymes with applications in diagnostics, bioremediation and cancer treatment. Despite the importance of these enzymes, they are still isolated from plant at low yields with different biochemical properties. Here we show the production of homogeneous glycoprotein species of recombinant horseradish peroxidase by using a P. pastoris platform strain in which OCH1 was deleted. This och1 knockout strain showed a growth impaired phenotype and considerable rearrangements of cell wall components, but nevertheless secreted more homogeneously glycosylated protein carrying mainly Man8 instead of Man10 N-glycans as a dominant core glycan structure at a volumetric productivity of 70% of the wildtype strain.
63 citations
TL;DR: The recombinant proteins caused chronic effects when fed, causing reductions in larval growth and food consumption by up to 60% and oral toxicity of chitinase was not increased by attaching GNA in the fusion protein, due to degradation in the larval gut, preventing GNA acting as a "carrier".
63 citations