Characterization and Diagnostic Potential of Foreign Epitope-Presenting Ty1 Virus-Like Particles Expressed in Escherichia coli and Pichia pastoris

2010 ◽  
Vol 18 (1) ◽  
pp. 52-62 ◽  
Author(s):  
Kerstin Uhde-Holzem ◽  
Rainer Fischer ◽  
Ulrich Commandeur
Keyword(s):  
Escherichia Coli ◽  
Pichia Pastoris ◽  
Virus Like Particles ◽  
Diagnostic Potential ◽  
Foreign Epitope

Production of Recombinant Human Trypsinogen in Escherichia Coli and Pichia Pastoris

2001 ◽  
pp. 339-346
Author(s):  
Hubertus Hohenblum ◽  
Stefan Naschberger ◽  
Robert Weik ◽  
Hermann Katinger ◽  
Diethard Mattanovich
Keyword(s):  
Escherichia Coli ◽  
Pichia Pastoris

Recombinant strains producing thermostable lipase from Thermomyces lanuginosus and their use in heterogeneous biocatalysis, including in the processes of low-temperature synthesis of esters

2021 ◽  
Vol 37 (5) ◽  
pp. 5-19
Author(s):  
M.B. Pykhtina ◽  
L.V. Perminova ◽  
G.A. Kovalenko
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Pichia Pastoris ◽  
Substrate Specificity ◽  
Carbon Aerogel ◽  
Operational Stability ◽  
Thermomyces Lanuginosus ◽  
Thermostable Lipase ◽  
Recombinant Strains ◽  
Heterogeneous Biocatalysts

Abstract-This work was devoted to the construction of recombinant strains Escherichia coli BL21 (DE3) and Pichia pastoris X33, producing a 1,3-specific thermostable lipase from Thermomyces lanuginosus. The sequences of two lipase genes were optimized for expression in bacteria and methylotrophic yeasts, then synthesized and cloned into the corresponding expression vectors. As a result of genetic engineering manipulations, E. coli and P. pastoris strains were constructed that efficiently produced recombinant lipase from T. lanuginosus, which accumulated in the cytoplasm in an amount of 30-40% of the total cellular protein. Recombinant P. pastoris clones secreted lipase into the nutrient medium at a concentration of at least 1 g/L. Lipases produced by the recombinant clones, designated as rE.coli/lip and rPichia/lip, respectively, contained a six-histidine sequence (-His6) in the C-terminal region. The resulting lipases were immobilized on/in solid inorganic supports in order to develop heterogeneous biocatalysts (HB) for the enzymatic conversion of triglycerides and fatty acids. The rPichia/lip enzyme was adsorbed on mesoporous silica and macroporous carbon aerogel. The properties of the prepared HB, their enzymatic activity, substrate specificity and operational stability were studied in the reaction of esterification of fatty acids with aliphatic alcohols in organic solvents at 20 ± 2°C. It was found that immobilized lipases had a relatively wide substrate specificity, as well as high operational stability, and the prepared HB almost completely retained their high esterifying activity for several tens of reaction cycles. Key words: Escherichia coli, Pichia pastoris, recombinant strains-producers, Thermomyces lanuginosus lipase gene, immobilization, biocatalysts, esterification The authors are grateful to V. L. Kuznetsov for the provided samples of carbon aerogel and A. V. Ryabchenko for gene-engineering manipulation aimed at obtaining the recombinant rE. coli strain, a producer of the rE.coli/lip enzyme. The work was carried out under the Project on Fundamental Research within the framework of a state assignment to the Institute for Catalysis "Catalysts and Processes of Renewable Raw Material Conversion" (no. 0239-2021-0005).

scholarly journals Expression of GA Coat Protein-Derived Mosaic Virus-Like Particles in Saccharomyces cerevisiae and Packaging in vivo of mRNAs into Particles

2012 ◽  
Vol 66 (6) ◽  
pp. 234-241
Author(s):  
Arnis Strods ◽  
Dagnija Argule ◽  
Indulis Cielens ◽  
Ludmila Jackeviča ◽  
Regīna Renhofa
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Coat Protein ◽  
Pichia Pastoris ◽  
Mosaic Virus ◽  
Expression Vector ◽  
Expression Systems ◽  
Coding Sequences ◽  
Yeast Pichia Pastoris ◽  
Virus Like Particles

Our previous research showed that the best yield of virus-like particles (VLPs) formed by RNA bacteriophage GA coat protein was obtained by expression in yeast Pichia pastoris, while other used expression systems in Saccharomyces cerevisiae gave much lower amounts of capsids. The main reasons to attempt further studies in Saccharomyces cerevisiae were to improve the yield of GA-based VLPs using constructs with optimised nucleotide triplets in coding sequences, and to exploit the possibilities of the two-promoter Gal1/Gal10 system of expression vector pESC-URA for production of the desired mosaic VLPs and for packaging of mRNAs into VLPs in vivo

scholarly journals Expression and self-assembly of Heterocapsa circularisquama RNA virus-like particles synthesized in Pichia pastoris

2012 ◽  
Vol 57 (25) ◽  
pp. 3288-3293 ◽  
Author(s):  
YuanZheng Wu ◽  
Wonduck Kim ◽  
Si-Wouk Kim ◽  
Chi-Yong Eom ◽  
HeTong Yang ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Self Assembly ◽  
Rna Virus ◽  
Virus Like Particles ◽  
Heterocapsa Circularisquama

Cloning, Expression, and Characterization of Siamese Crocodile (Crocodylus siamensis) Hemoglobin from Escherichia coli and Pichia pastoris

2016 ◽  
Vol 35 (4) ◽  
pp. 256-268 ◽  
Author(s):  
Preeyanan Anwised ◽  
Nisachon Jangpromma ◽  
Theeranan Temsiripong ◽  
Rina Patramanon ◽  
Sakda Daduang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pichia Pastoris ◽  
Crocodylus Siamensis

Escherichia coli-based cell free production of flagellin and ordered flagellin display on virus-like particles

2013 ◽  
Vol 110 (8) ◽  
pp. 2073-2085 ◽  
Author(s):  
Yuan Lu ◽  
John P. Welsh ◽  
Wei Chan ◽  
James R. Swartz
Keyword(s):  
Escherichia Coli ◽  
Virus Like Particles

Human papillomavirus L1 protein expressed in Escherichia coli self-assembles into virus-like particles that are highly immunogenic

2016 ◽  
Vol 220 ◽  
pp. 97-103 ◽  
Author(s):  
Yumei Chen ◽  
Yunchao Liu ◽  
Gaiping Zhang ◽  
Aiping Wang ◽  
Ziming Dong ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Human Papillomavirus ◽  
Virus Like Particles ◽  
L1 Protein

A System for Dual Protein Expression in Pichia pastoris and Escherichia coli

2000 ◽  
Vol 20 (3) ◽  
pp. 372-378 ◽  
Author(s):  
Angelika Lueking ◽  
Caterina Holz ◽  
Christine Gotthold ◽  
Hans Lehrach ◽  
Dolores Cahill
Keyword(s):  
Escherichia Coli ◽  
Pichia Pastoris ◽  
Protein Expression
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