Results 11 to 20 of about 47,430 (223)

Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production [PDF]

Applied Microbiology and Biotechnology, 2014
Pichia pastoris is an established protein expression host mainly applied for the production of biopharmaceuticals and industrial enzymes. This methylotrophic yeast is a distinguished production system for its growth to very high cell densities, for the ...
Harald Pichler, Helmut Schwab, Melanie Hirz, Mudassar Ahmad   +3 more
core   +3 more sources

Low-cost media statistical design for laccase rPOXA 1B production in P. pastoris. [PDF]

Heliyon, 2020
Laccases (E.C. 1.10.3.2) are multicopper oxidases of great importance in the industry due to their non-specificity and high oxidative potential. Laccases are useful to bleach synthetic dyes, oxidize phenolic compounds and degrade pesticides, among others. Hence, the objective of this work was to optimize low cost culture media for recombinant (rPOXA 1B)
Ardila-Leal LD, Alvarado-Ramírez MF, Gutiérrez-Rojas IS, Poutou-Piñales RA, Quevedo-Hidalgo B, Pérez-Flórez A, Pedroza-Rodríguez AM.   +6 more
europepmc   +5 more sources

Codon usage bias regulates gene expression and protein conformation in yeast expression system P. pastoris. [PDF]

Microb Cell Fact, 2021
Abstract Background Protein synthesis is one of the extremely important anabolic pathways in the yeast expression system Pichia pastoris. Codon optimization is a commonly adopted strategy for improved protein expression, although unexpected failures did appear sometimes waiting for further exploration.
Xu Y, Liu K, Han Y, Xing Y, Zhang Y, Yang Q, Zhou M.   +6 more
europepmc   +5 more sources

Media improvement for 10 L bioreactor production of rPOXA 1B laccase by P. pastoris. [PDF]

3 Biotech, 2019
In this work, we statistically improved culture media for rPOXA 1B laccase production, expressed in Pichia pastoris containing pGAPZαA-LaccPost-Stop construct and assayed at 10 L bioreactor production scale (6 L effective work volume). The concentrated enzyme was evaluated for temperature and pH stability and kinetic parameter, characterized by ...
Ardila-Leal LD, Albarracín-Pardo DA, Rivera-Hoyos CM, Morales-Álvarez ED, Poutou-Piñales RA, Cardozo-Bernal AM, Quevedo-Hidalgo BE, Pedroza-Rodríguez AM, Díaz-Rincón DJ, Rodríguez-López A, Alméciga-Díaz CJ, Cuervo-Patiño CL.   +11 more
europepmc   +4 more sources

A Cytoplasm to Vacuole Targeting Pathway inP. pastoris [PDF]

Autophagy, 2007
The cytoplasm-to-vacuole targeting (Cvt) pathway of Saccharomyces cerevisiae delivers aminopeptidase I (Ape1) from the cytosol to the vacuole, bypassing the normal secretory route. The Cvt pathway, although well-studied, was known only in S. cerevisiae. We demonstrate its existence in the methylotrophic yeast, Pichia pastoris, where it also delivers P.
Farré, Jean-Claude, Vidal, Jason, Subramani, Suresh   +2 more
openaire   +3 more sources

Small P particles formed by the Taiwan-native norovirus P domain overexpressed in Komagataella pastoris [PDF]

Applied Microbiology and Biotechnology, 2018
The protrusion (P) domain of the major structural protein VP1 of norovirus (NoV) is critical for the host's immune response and receptor binding. Most heterologous P domains expressed in Escherichia coli or Komagataella pastoris (formally known as Pichia pastoris) form P particles consisting of 24 P monomers formed through intermolecular contact in the
Yu-Ling Chen, Pey-Jium Chang, Ching-Tsan Huang   +2 more
openaire   +2 more sources

Enzymatic Degradation of Aromatic and Aliphatic Polyesters by P. pastoris Expressed Cutinase 1 from Thermobifida cellulosilytica. [PDF]

Front Microbiol, 2017
To study hydrolysis of aromatic and aliphatic polyesters cutinase 1 from Thermobifida cellulosilytica (Thc_Cut1) was expressed in P. pastoris. No significant differences between the expression of native Thc_Cut1 and of two glycosylation site knock out mutants (Thc_Cut1_koAsn and Thc_Cut1_koST) concerning the total extracellular protein concentration ...
Gamerith C, Vastano M, Ghorbanpour SM, Zitzenbacher S, Ribitsch D, Zumstein MT, Sander M, Herrero Acero E, Pellis A, Guebitz GM.   +9 more
europepmc   +7 more sources

Labeling of peroxisomes with green fluorescent protein in living P. pastoris cells. [PDF]

Journal of Histochemistry & Cytochemistry, 1996
We exploited the light-activated fluorescent properties of the green fluorescent protein (GFP) of the jellyfish Aequorea victoria for studies on the peroxisomal sorting of polypeptides. GFP and GFP-SKL (containing a C-terminal, tripeptide peroxisomal targeting signal, SKL) were expressed from a methanol-inducible, alcohol oxidase (AOX1) promoter in ...
E Z, Monosov, T J, Wenzel, G H, Lüers, J A, Heyman, S, Subramani   +4 more
openaire   +2 more sources

Compact multi-enzyme pathways in P. pastoris

Chemical Communications, 2015
2A peptides enabling the coordinate expression of nine genes in P. pastoris represent a valuable tool for pathway construction and engineering.
Geier, Martina; Fauland, Pia; Vogl, Thomas; Glieder, Anton   +4 more
openaire   +3 more sources

Expression of an anti-CD33 single-chain antibody by Pichia pastoris [PDF]

, 2005
CD33 is a cell surface glycoprotein expressed on cells of myelomonocytic lineage, leukaemic cells, but not haematopoietic stem cells. By virtue of its expression pattern, CD33 has become a popular target for new immunotherapeutic approaches to treat ...
Emberson, Louise M., Trivett, Amanda J., Blower, Philip J., Nicholls, Peter J.   +3 more
core   +1 more source