Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2018 Apr 29;6(2):38.
doi: 10.3390/microorganisms6020038.

Comparison of Yeasts as Hosts for Recombinant Protein Production

Affiliations
Review

Comparison of Yeasts as Hosts for Recombinant Protein Production

Antonio Milton Vieira Gomes et al. Microorganisms. .

Abstract

Recombinant protein production emerged in the early 1980s with the development of genetic engineering tools, which represented a compelling alternative to protein extraction from natural sources. Over the years, a high level of heterologous protein was made possible in a variety of hosts ranging from the bacteria Escherichia coli to mammalian cells. Recombinant protein importance is represented by its market size, which reached $1654 million in 2016 and is expected to reach $2850.5 million by 2022. Among the available hosts, yeasts have been used for producing a great variety of proteins applied to chemicals, fuels, food, and pharmaceuticals, being one of the most used hosts for recombinant production nowadays. Historically, Saccharomyces cerevisiae was the dominant yeast host for heterologous protein production. Lately, other yeasts such as Komagataella sp., Kluyveromyces lactis, and Yarrowia lipolytica have emerged as advantageous hosts. In this review, a comparative analysis is done listing the advantages and disadvantages of using each host regarding the availability of genetic tools, strategies for cultivation in bioreactors, and the main techniques utilized for protein purification. Finally, examples of each host will be discussed regarding the total amount of protein recovered and its bioactivity due to correct folding and glycosylation patterns.

Keywords: Kluyveromyces lactis; Komagataella phaffii; Saccharomyces cerevisiae; Yarrowia lipolytica; recombinant protein; yeast.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Main aspects to be considered for recombinant protein production in yeasts.
Figure 2
Figure 2
Recombinant protein glycosylation pattern in yeasts and mammalian cells.
Figure 3
Figure 3
Cultivation strategies choice based on the promoter utilized for recombinant gene expression.

References

    1. Baeshen N.A., Baeshen M.N., Sheikh A., Bora R.S., Ahmed M.M.M., Ramadan H.A.I., Saini K.S., Redwan E.M. Cell factories for insulin production. Microb. Cell Factories. 2014;13:14. doi: 10.1186/s12934-014-0141-0. - DOI - PMC - PubMed
    1. Protein Expression Market worth 2850.5 Million USD by 2022. [(accessed on 26 April 2018)]; Available online: https://www.marketsandmarkets.com/PressReleases/protein-expression.asp.
    1. Lagassé H.A.D., Alexaki A., Simhadri V.L., Katagiri N.H., Jankowski W., Sauna Z.E., Kimchi-Sarfaty C. Recent advances in (therapeutic protein) drug development. F1000Research. 2017;6:113. doi: 10.12688/f1000research.9970.1. - DOI - PMC - PubMed
    1. Jia B., Jeon C.O. High-throughput recombinant protein expression in Escherichia coli: Current status and future perspectives. Open Biol. 2016;6:160196. doi: 10.1098/rsob.160196. - DOI - PMC - PubMed
    1. Boettner M., Prinz B., Holz C., Stahl U., Lang C. High-throughput screening for expression of heterologous proteins in the yeast Pichia pastoris. J. Biotechnol. 2002;99:51–62. doi: 10.1016/S0168-1656(02)00157-8. - DOI - PubMed