Expression of Recombinant Human Tropoelastin inSaccharomyces cerevisiae Containing a Synthetic Gene with a High Codon Adaptation Index Coupled to theSUC2 Invertase Signal Sequence

Toonkool, Prachumporn; Weiss, Anthony S.

doi:10.1002/1521-3846(200105)21:2<189::aid-abio189>3.0.co;2-z

Cited by 8 publications

(3 citation statements)

References 12 publications

(17 reference statements)

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“…Unlike collagen, tropoelastin is encoded by a single gene that when expressed is spliced to produce different isoforms of tropoelastin proteins to meet the functional requirements in the different tissues. This gene has been expressed in E. coli, S. cerevisiae, and P. pastoris systems, nonetheless, protein expression can be challenging due to the highly repetitive gene sequence of tropoelastin that is prone to mutational events, lack of protein secretion, and also reduced levels of protein expression [163,164]. To address this issue, attempts have been made to express elastin-like proteins (Table 2) using synthetic designed nonrepetitive DNA sequences and/or peptide repeats.…”

Section: Structural Proteinsmentioning

confidence: 99%

Precision Fermentation as an Alternative to Animal Protein, a Review

Knychala,

Boing,

Ienczak

et al. 2024

Preprint

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The global food production system faces several challenges, including significant environmental impacts due to traditional agricultural practices. The rising demands of consumers for food products that are safe, healthy, and have animal welfare standards have led to an increased interest in alternative proteins and the development of the cellular agriculture field. Within this innovative field, precision fermentation emerges as a promising technological solution to produce proteins with reduced ecological footprints. This review provides a summary of the environmental impacts related to the current global food production, and explore how precision fermentation can contribute to address these issues. Additionally, we will report on the main animal-derived proteins produced by precision fermentation, with a particular focus on those used in the food and nutraceutical industries. The general principles of precision fermentation will be explained, including strain and bioprocess optimization. Examples of efficient recombinant protein production by bacteria and yeasts, such as milk proteins, egg-white proteins, structural and flavoring proteins, will also be addressed, along with case examples of companies producing these recombinant proteins in a commercial scale. Through these examples, we will explore how precision fermentation supports sustainable food production and holds the potential for significant innovations in the sector.

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Section: Structural Proteinsmentioning

confidence: 99%

Precision Fermentation as an Alternative to Animal Protein, a Review

Knychala,

Boing,

Ienczak

et al. 2024

Preprint

View full text Add to dashboard Cite

show abstract

“…Unlike collagen, tropoelastin is encoded by a single gene that when expressed is spliced to produce different isoforms of tropoelastin proteins to meet the functional requirements in the different tissues. This gene has been expressed in E. coli, S. cerevisiae, and K. phaffii systems, nonetheless, protein expression can be challenging due to the highly repetitive gene sequence of tropoelastin that is prone to mutational events, lack of protein secretion, and also reduced levels of protein expression [196,197]. To address this issue, attempts have been made to express elastin-like proteins (Table 2) using synthetic designed nonrepetitive DNA sequences and/or peptide repeats.…”

Section: Structural Proteinsmentioning

confidence: 99%

Precision Fermentation as an Alternative to Animal Protein, a Review

Knychala,

Boing,

Ienczak

et al. 2024

Fermentation

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The global food production system faces several challenges, including significant environmental impacts due to traditional agricultural practices. The rising demands of consumers for food products that are safe, healthy, and have animal welfare standards have led to an increased interest in alternative proteins and the development of the cellular agriculture field. Within this innovative field, precision fermentation has emerged as a promising technological solution to produce proteins with reduced ecological footprints. This review provides a summary of the environmental impacts related to the current global food production, and explores how precision fermentation can contribute to address these issues. Additionally, we report on the main animal-derived proteins produced by precision fermentation, with a particular focus on those used in the food and nutraceutical industries. The general principles of precision fermentation will be explained, including strain and bioprocess optimization. Examples of efficient recombinant protein production by bacteria and yeasts, such as milk proteins, egg-white proteins, structural and flavoring proteins, will also be addressed, along with case examples of companies producing these recombinant proteins at a commercial scale. Through these examples, we explore how precision fermentation supports sustainable food production and holds the potential for significant innovations in the sector.

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“…Aspergillus nidulans [93], tobacco plants [94], and S. cerevisiae [95]. In all these studies the ELPs were produced intracellularly.…”

Section: Elastin-like Proteinsmentioning

confidence: 99%

Production of protein‐based polymers in Pichia pastoris

Werten

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A long-sought objective in material science is the development of polymers with controlled monomer sequence [1, 2]. Although progress has been made in synthetic chemistry [3], the level of control evident in natural sequential polymers such as DNA and proteins is unparalleled. These biological macromolecules feature a defined molecular size, as well as a controlled sequence of the nucleotide or amino acid monomers. Proteins fold into a three-dimensional structure defined by their primary sequence, resulting in unique properties. From 20 different amino acid monomers, nature has created an awe-inspiring wealth of different proteins, including enzymes, antibodies, and peptide hormones, as well as nonbioactive proteins with a structure-forming, rheological, or colloidal function. The latter category includes proteins such as collagen and elastin that fulfill a major role in the structure of various tissues, and silks used in animal architecture such as silkworm cocoons and spider webs (for more information see Section 9.1 of the General discussion). These proteins typically feature highly repetitive sequences with biased amino acid composition, and can often reversibly self-assemble into supramolecular structures through the formation of noncovalent bonds. The natural materials derived from them display remarkable toughness, elasticity, and other properties that have inspired material scientists to mimic them using modern protein engineering. These so-called protein-based polymers, or protein polymers for short, are produced as heterologous proteins in a suitable host, just like enzymes and other proteins, although their highly repetitive sequence, biased amino acid composition, and physicochemical properties do present additional difficulty. The genes encoding natural protein polymers are sometimes used, but more often genes are synthesized that encode simplified mimics, or even completely de novo-designed protein polymers [4-6]. Multifunctional block copolymers can be prepared by combining different polymer types into one molecule [1, 2, 7-9]. Ever since the pioneering work by Cappello and Ferrari of Protein Polymer Technologies [10, 11], Escherichia coli has by far been the most widely used production host for protein polymers. This workhorse of protein engineering is genetically very well accessible, and offers fast growth and efficient low-cost production [12]. Several other hosts have been used for the production of protein polymers, including plants, insect cells, transgenic animals, Aspergillus nidulans, Saccharomyces cerevisiae,

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Expression of Recombinant Human Tropoelastin inSaccharomyces cerevisiae Containing a Synthetic Gene with a High Codon Adaptation Index Coupled to theSUC2 Invertase Signal Sequence

Cited by 8 publications

References 12 publications

Precision Fermentation as an Alternative to Animal Protein, a Review

Precision Fermentation as an Alternative to Animal Protein, a Review

Precision Fermentation as an Alternative to Animal Protein, a Review

Production of protein‐based polymers in Pichia pastoris

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