Safety evaluation of a lipase enzyme preparation, expressed in Pichia pastoris, intended for use in the degumming of edible vegetable oil

Ciofalo, Vince; Barton, Nelson; Kreps, Joel; Coats, Isabelle; Shanahan, Diane

doi:10.1016/j.yrtph.2006.02.001

Cited by 52 publications

(18 citation statements)

References 20 publications

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“…A major breakthrough was the publication of detailed genome sequences of the original SCP production strain CBS7435 (Küberl et al 2011), the first host strain developed for heterologous protein expression GS115 (De Schutter et al 2009), as well as of the related P. pastoris DSMZ 70382 strain (Mattanovich et al 2009b). Equally important breakthroughs for the commercial application of the P. pastoris cell factory were the Food and Drug Administration (FDA) GRAS (generally recognized as safe) status for a protein used in animal feed, phospholipase C (Ciofalo et al 2006), and the FDA approval of a recombinant biopharmaceutical product, Kalbitor®, a kallikrein inhibitor (Thompson 2010). …”

Section: Introductionmentioning

confidence: 99%

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

Ahmad

Hirz

Pichler

et al. 2014

Appl Microbiol Biotechnol

807

564

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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 available strong and tightly regulated promoters, and for the options to produce gram amounts of recombinant protein per litre of culture both intracellularly and in secretory fashion. However, not every protein of interest is produced in or secreted by P. pastoris to such high titres. Frequently, protein yields are clearly lower, particularly if complex proteins are expressed that are hetero-oligomers, membrane-attached or prone to proteolytic degradation. The last few years have been particularly fruitful because of numerous activities in improving the expression of such complex proteins with a focus on either protein engineering or on engineering the protein expression host P. pastoris. This review refers to established tools in protein expression in P. pastoris and highlights novel developments in the areas of expression vector design, host strain engineering and screening for high-level expression strains. Breakthroughs in membrane protein expression are discussed alongside numerous commercial applications of P. pastoris derived proteins.

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Section: Introductionmentioning

confidence: 99%

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

Ahmad

Hirz

Pichler

et al. 2014

Appl Microbiol Biotechnol

807

564

View full text Add to dashboard Cite

show abstract

“…In this work, we look for a safe vaccine with higher acceptance. To this end, instead of a DNA-based vaccine using an attenuated bacterium as carrier, we use purified protein Tc52 produced in Pichia pastoris , an organism with GRAS (Generally Recognized As Safe) status conferred by the USA FDA [21, 22]. …”

Section: Introductionmentioning

confidence: 99%

Immunization with Tc52 or its amino terminal domain adjuvanted with c-di-AMP induces Th17+Th1 specific immune responses and confers protection against Trypanosoma cruzi

et al. 2017

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The development of new adjuvants enables fine modulation of the elicited immune responses. Ideally, the use of one or more adjuvants should result in the induction of a protective immune response against the specific pathogen. We have evaluated the immune response and protection against Trypanosoma cruzi infection in mice vaccinated with recombinant Tc52 or its N- and C-terminal domains (NTc52 and CTc52) adjuvanted either with the STING (Stimulator of Interferon Genes) agonist cyclic di-AMP (c-di-AMP), a pegylated derivative of α-galactosylceramide (αGC-PEG), or oligodeoxynucleotides containing unmethylated CpG motifs (ODN-CpG). All groups immunized with the recombinant proteins plus adjuvant: Tc52+c-di-AMP, NTc52+c-di-AMP, CTc52+c-di-AMP, NTc52+c-di-AMP+αGC-PEG, NTc52+CpG, developed significantly higher anti-Tc52 IgG titers than controls. Groups immunized with c-di-AMP and Tc52, NTc52 or CTc52 showed the highest Tc52-specific IgA titers in nasal lavages. All groups immunized with the recombinant proteins plus adjuvant developed a strong specific cellular immune response in splenocytes and lymph node cells with significant differences for groups immunized with c-di-AMP and Tc52, NTc52 or CTc52. These groups also showed high levels of Tc52-specific IL-17 and IFN-γ producing cells, while NTc52+CpG group only showed significant difference with control in IFN-γ producing cells. Groups immunized with c-di-AMP and Tc52, NTc52 or CTc52 developed predominantly a Th17 and Th1immune response, whereas for NTc52+CpG it was a dominant Th1 response. It was previously described that αGC-PEG inhibits Th17 differentiation by activating NKT cells. Thus, in this work we have also included a group immunized with both adjuvants (NTc52+c-di-AMP+αGC-PEG) with the aim to modulate the Th17 response induced by c-di-AMP. This group showed a significant reduction in the number of Tc52-specific IL-17 producing splenocytes, as compared to the group NTc52+c-di-AMP, which has in turn correlated with a reduction in protection against infection. These results suggest that the Th17 immune response developed after immunizing with NTc52+c-di-AMP could have a protective role against T. cruzi infection. Groups NTc52+c-di-AMP, Tc52+c-di-AMP and NTc52PB, were the ones that showed better protection against infection with lower parasitemia and weight loss, and higher survival.

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“…The test article samples were also tested for and shown to be free of antimicrobial activity and mycotoxins. Mycotoxins were analysed using high-performance liquid chromatography for aflatoxins and ochratoxin A and thin-layer chromatography for T-2 toxin and sterigmatocystin (Ciofalo et al, 2006). The limits of detection for the mycotoxins tested were as follows: aflatoxin B1, 1.0 μg/kg; aflatoxin B2, 1.0 μg/kg; aflatoxin G1, 1.0 μg/kg; aflatoxin G2, 1.0 μg/kg; ochratoxin A, 2 μg/kg; T-2 toxin, 0.1 mg/kg; and sterigmatocystin, 200 μg/kg.…”

Section: 2mentioning

confidence: 99%

Joint FAO/WHO Expert Committee on Food Additives (JECFA)

Sagert¹

2008

Encyclopedia of Global Health

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Safety evaluation of a lipase enzyme preparation, expressed in Pichia pastoris, intended for use in the degumming of edible vegetable oil

Cited by 52 publications

References 20 publications

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

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

Immunization with Tc52 or its amino terminal domain adjuvanted with c-di-AMP induces Th17+Th1 specific immune responses and confers protection against Trypanosoma cruzi

Joint FAO/WHO Expert Committee on Food Additives (JECFA)

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