Comparison of Yeasts as Hosts for Recombinant Protein Production
Abstract
:1. Introduction
2. Availability of Genetic Tools.
2.1. DNA Assembly Methods
2.2. Genetic Elements Applied to Recombinant Protein Production
2.3. Vector Availability
2.4. Genome Editing Techniques
3. Post-Translational Modifications Related to Bioactive Recombinant Proteins
4. Yeast Secretion Factors
5. Cultivation Strategies for Maximization of Recombinant Proteins in Bioreactors
5.1. Recombinant Genes under the Control of Constitutive Promoters
5.2. Recombinant Genes under the Control of Inducible Promoters
6. Perspectives in Recombinant Protein Production
Acknowledgments
Conflicts of Interest
References
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Host. | Constitutive Promoters | Inducible Promoters |
---|---|---|
S. cerevisiae | ADH1, GAPDH, PGK1, TPI, ENO, PYK1, TEF | GAL1-10, CUP1, ADH2 |
K. lactis | PGK | LAC4, ADH4 |
Y. lipolytica | TEF, RPS7, XPR2/hp4d | POX2, POT1, ICL1 |
K. phaffii | GAP, TEF, PGK, YPT1 | AOX1, FLD1, PEX8 |
Yeast | Recombinant Protein | Protein secreted | Secretion factor | Secretion Signal Source | Ref. |
---|---|---|---|---|---|
K. phaffii | EGFP | -- a | HBFI | Trichoderma reesei Hydrophobin | [112] |
Y. lipolytica | Invertase | -- | XPR2 pre c | Y. lipolytica Alkaline extracellular protease precursor | [113] |
Y. lipolytica | Galactanase I | 3 mg/L | XPR2 pre c | Y. lipolytica Alkaline extracellular protease precursor | [114] |
Y. lipolytica | α-amylase | -- | XPR2 pre-pro c | Y. lipolytica Alkaline extracellular protease precursor | [115] |
Y. lipolytica | Aspartic proteinase II | -- | Hybrid LIP2/XPR2 pre-pro c | Y. lipolytica Alkaline extracellular protease precursor | [116] |
K. lactis | α-amylase | 0.527 U/mL | KT | Synthetic | [39] |
K. lactis | Insulin precursor | 30 mg/L | α-MF | S. cerevisiae α-mating factor | [117] |
K. lactis | a-galactosidase | 2 mg/L | SUC2 pre | S. cerevisiae invertase | [118] |
K. lactis | Growth hormone | -- | PHO5 | K. lactis acid phosphatase | [119] |
K. lactis | Serum albumin (HSA) | 3 g/L | HSA pre-pro | - | [120] |
K. phaffii | Horseradish peroxidase | -- | α-MF | S. cerevisiae α-mating factor | [111] |
K. phaffii | α1-antitrypsin | -- | SUC2 | S. cerevisiae invertase | [116] |
K. phaffii | α1-antitrypsin | -- | PIR1 | Proteins with internal repeats (PIR) from K. phaffii | [39] |
K. phaffii | Porcine Pepsinogen | -- | PHO1 | K. phaffii acid phosphatase | [117] |
K. phaffii | α-amylase | 2.5 g/L | SUC2 | S. cerevisiae invertase | [118] |
K. phaffii | α-amylase | 240 ug/mL | pGKL | PGKL killer protein | [51] |
K. phaffii | EGFP | -- | SCW, DSE, and EXG | Endogenous signal peptides | [121] |
K. phaffii | EGFP | -- | PIR1 | Proteins with internal repeats (PIR) from K. phaffii | [39] |
S. cerevisiae | β-galactosidase | 0.8 b | AGA2 | S. cerevisiae Adhesion subunit of a-agglutinin | [122] |
S. cerevisiae | β-galactosidase | 0.9 b | EXG | S. cerevisiae Exo-1,3-B-Glucanase | |
S. cerevisiae | β-galactosidase | 0.9 b | α-MF | S. cerevisiae α-mating factor | |
S. cerevisiae | β-galactosidase | 0.9 b | CRH | S. cerevisiae Chitin trans-glycosylase | |
S. cerevisiae | β-galactosidase | 0.65 b | PLB | S. cerevisiae Phospholipase B | |
S. cerevisiae | β-galactosidase | 0.85 b | SUN | Cell wall protein related to glucanases of S. cerevisiae | |
S. cerevisiae | Hen Lysozyme | 13 mg/L | α-MF | S. cerevisiae α-mating factor | [123] |
S. cerevisiae | Hen Lysozyme | 2.6 mg/L | KILM1 | S. cerevisiae Killer toxin type 1 | |
S. cerevisiae | Hen Lysozyme | 2.1 mg/L | PHO1 | S. cerevisiae Acid phosphatase | |
S. cerevisiae | Hen Lysozyme | 2.0 mg/L | SUC2 | S. cerevisiae invertase |
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Vieira Gomes, A.M.; Souza Carmo, T.; Silva Carvalho, L.; Mendonça Bahia, F.; Parachin, N.S. Comparison of Yeasts as Hosts for Recombinant Protein Production. Microorganisms 2018, 6, 38. https://doi.org/10.3390/microorganisms6020038
Vieira Gomes AM, Souza Carmo T, Silva Carvalho L, Mendonça Bahia F, Parachin NS. Comparison of Yeasts as Hosts for Recombinant Protein Production. Microorganisms. 2018; 6(2):38. https://doi.org/10.3390/microorganisms6020038
Chicago/Turabian StyleVieira Gomes, Antonio Milton, Talita Souza Carmo, Lucas Silva Carvalho, Frederico Mendonça Bahia, and Nádia Skorupa Parachin. 2018. "Comparison of Yeasts as Hosts for Recombinant Protein Production" Microorganisms 6, no. 2: 38. https://doi.org/10.3390/microorganisms6020038
APA StyleVieira Gomes, A. M., Souza Carmo, T., Silva Carvalho, L., Mendonça Bahia, F., & Parachin, N. S. (2018). Comparison of Yeasts as Hosts for Recombinant Protein Production. Microorganisms, 6(2), 38. https://doi.org/10.3390/microorganisms6020038