Selection of the Optimal Yeast Host for the Synthesis of Recombinant Enzymes

Bischoff, Felix; Giersberg, Martin; Matthes, Falko; Schwalenberg, Tobias; Worch, Sebastian; Kunze, Gotthard

doi:10.1007/978-1-4939-9024-5_4

Cited by 4 publications

(5 citation statements)

References 43 publications

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“…phaffii , Kluyveromyces lactis , Chlamydomonas reinhardtii , and to a lesser extent, Ogataea polymorpha ( Hansenula polymorpha ). Many different organisms within the scope of this review have been exploited for recombinant protein expression (Table 1), with each having their own unique characteristics (e.g., expression mechanisms, tolerance to salt, and optimal growth temperature range) that can make them more suitable for specific applications (Bischoff et al., 2019; Rebello et al., 2018). This section will cover several main yeast and algal hosts, and include a final subsection on potential up‐and‐coming expression hosts, with a focus placed on research from the last 10 years.…”

Section: Expression Hostsmentioning

confidence: 99%

Precision cellular agriculture: The future role of recombinantly expressed protein as food

Dupuis

Cheung

Newman

et al. 2022

Comp Rev Food Sci Food Safe

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Cellular agriculture is a rapidly emerging field, within which cultured meat has attracted the majority of media attention in recent years. An equally promising area of cellular agriculture, and one that has produced far more actual food ingredients that have been incorporated into commercially available products, is the use of cellular hosts to produce soluble proteins, herein referred to as precision cellular agriculture (PCAg). In PCAg, specific animal‐ or plant‐sourced proteins are expressed recombinantly in unicellular hosts—the majority of which are yeast—and harvested for food use. The numerous advantages of PCAg over traditional agriculture, including a smaller carbon footprint and more consistent products, have led to extensive research on its utility. This review is the first to survey proteins currently being expressed using PCAg for food purposes. A growing number of viable expression hosts and recent advances for increased protein yields and process optimization have led to its application for producing milk, egg, and muscle proteins; plant hemoglobin; sweet‐tasting plant proteins; and ice‐binding proteins. Current knowledge gaps present research opportunities for optimizing expression hosts, tailoring posttranslational modifications, and expanding the scope of proteins produced. Considerations for the expansion of PCAg and its implications on food regulation, society, ethics, and the environment are also discussed. Considering the current trajectory of PCAg, food proteins from any biological source can likely be expressed recombinantly and used as purified food ingredients to create novel and tailored food products.

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Section: Expression Hostsmentioning

confidence: 99%

Precision cellular agriculture: The future role of recombinantly expressed protein as food

Dupuis

Cheung

Newman

et al. 2022

Comp Rev Food Sci Food Safe

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“…Transformation procedures of E. coli and B. raffinosifermentans were performed according to Böer et al (2009a) and Bischoff et al (2019). Plasmid DNA isolation and DNA restriction digests were carried out as described by Wartmann et al (2002).…”

Section: Transformation and Isolation Procedures Of Nucleic Acidsmentioning

confidence: 99%

Characterization of Catechol-1,2-Dioxygenase (Acdo1p) From Blastobotrys raffinosifermentans and Investigation of Its Role in the Catabolism of Aromatic Compounds

et al. 2022

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Gallic acid, protocatechuic acid, catechol, and pyrogallol are only a few examples of industrially relevant aromatics. Today much attention is paid to the development of new microbial factories for the environmentally friendly biosynthesis of industrially relevant chemicals with renewable resources or organic pollutants as the starting material. The non–conventional yeast, Blastobotrys raffinosifermentans, possesses attractive properties for industrial bio-production processes such as thermo- and osmotolerance. An additional advantage is its broad substrate spectrum, with tannins at the forefront. The present study is dedicated to the characterization of catechol-1,2-dioxygenase (Acdo1p) and the analysis of its function in B. raffinosifermentans tannic acid catabolism. Acdo1p is a dimeric protein with higher affinity for catechol (KM = 0.004 ± 0.001 mM, kcat = 15.6 ± 0.4 s–1) than to pyrogallol (KM = 0.1 ± 0.02 mM, kcat = 10.6 ± 0.4 s–1). It is an intradiol dioxygenase and its reaction product with catechol as the substrate is cis,cis-muconic acid. B. raffinosifermentans G1212/YIC102-AYNI1-ACDO1-6H, which expresses the ACDO1 gene under the control of the strong nitrate-inducible AYNI1 promoter, achieved a maximum catechol-1,2-dioxygenase activity of 280.6 U/L and 26.9 U/g of dry cell weight in yeast grown in minimal medium with nitrate as the nitrogen source and 1.5% glucose as the carbon source. In the same medium with glucose as the carbon source, catechol-1,2-dioxygenase activity was not detected for the control strain G1212/YIC102 with ACDO1 expression under the regulation of its respective endogenous promoter. Gene expression analysis showed that ACDO1 is induced by gallic acid and protocatechuic acid. In contrast to the wild-type strain, the B. raffinosifermentans strain with a deletion of the ACDO1 gene was unable to grow on medium supplemented with gallic acid or protocatechuic acid as the sole carbon source. In summary, we propose that due to its substrate specificity, its thermal stability, and its ability to undergo long-term storage without significant loss of activity, B. raffinosifermentans catechol-1,2-dioxygenase (Acdo1p) is a promising enzyme candidate for industrial applications.

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“…including Yarrowia lipolytica, Saccharomyces cerevisiae, Arxula adeninivorans, Pichia pastoris, Hansenula polymorpha, Debaryomyces hansenii, Schwanniomyces occidentalis, and Yarrowia lipolytica (Bischoff et al, 2019).…”

Section: Challeng E S In the B I Opro Ce Ss Ing And Appli C Ati On mentioning

confidence: 99%

“…These include fast growth kinetics, high cell density, readily available and inexpensive growth media, and fast and easy DNA transformation (Levine, Gregorio, Jewett, Watts, & Oza, 2019; Menacho‐Melgar et al., 2020; Rosano & Ceccarelli, 2014; Rosano, Morales, & Ceccarelli, 2019; Seyfi, Babaeipour, Mofid, & Kahaki, 2019). A number of host yeast strains for recombinant production of proteins have also been reported, including Yarrowia lipolytica , Saccharomyces cerevisiae, Arxula adeninivorans, Pichia pastoris , Hansenula polymorpha, Debaryomyces hansenii, Schwanniomyces occidentalis, and Yarrowia lipolytica (Bischoff et al., 2019).…”

Section: Challenges In the Bioprocessing And Application Of Extremozymentioning

confidence: 99%

Revisiting the scope and applications of food enzymes from extremophiles

Akanbi

Agyei

2020

J. Food Biochem.

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Selection of the Optimal Yeast Host for the Synthesis of Recombinant Enzymes

Cited by 4 publications

References 43 publications

Precision cellular agriculture: The future role of recombinantly expressed protein as food

Precision cellular agriculture: The future role of recombinantly expressed protein as food

Characterization of Catechol-1,2-Dioxygenase (Acdo1p) From Blastobotrys raffinosifermentans and Investigation of Its Role in the Catabolism of Aromatic Compounds

Revisiting the scope and applications of food enzymes from extremophiles

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