| Protein name |
Ovalbumin |
| Host compatibility |
Trichoderma reesei |
| Yield |
2 g/L (Aro et al., 2023)
|
| Scale (in specific example) |
Lab scale in bioreactor (Aro et al., 2023)
|
| Biggest scale product has been develloped in this organism |
Pilot or industrial scale (Onego Bio & the EVERY Compnay) |
| Regulatory status in Europe |
Not allowed |
| Regulatory status in other parts of the world |
Has been filed for FDA GRAS approval in the US. Not allowed in Canada
|
| Companies producing this protein in this organism |
|
| Extra/remark |
|
| Publications/references |
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Aro, N., Ercili-Cura, D., Andberg, M., Silventoinen, P., Lille, M., Hosia, W., Nordlund, E., & Landowski, C. P. (2023). Production of bovine beta-lactoglobulin and hen egg ovalbumin by Trichoderma reesei using precision fermentation technology and testing of their techno-functional properties. Food Research International, 163, 112131. https://doi.org/10.1016/j.foodres.2022.112131
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Beck, F., Noll, P., Schweiggert-Weisz, U., & Henkel, M. (2025). Scientific and technological challenges of recombinant egg protein production. BMC Biotechnology. https://doi.org/10.1186/s12896-025-01002-3
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Nielsen, M., Meyer, A., & Arnau, J. (2024). The Next Food Revolution Is Here: Recombinant Microbial Production of Milk and Egg Proteins by Precision Fermentation. Annual Review of Food Science and Technology, 15(1), 173–187. https://doi.org/10.1146/annurev-food-072023-034256
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Rostamabadi, H., Chaudhary, V., Chhikara, N., Sharma, N., Nowacka, M., Demirkesen, I., Rathnakumar, K., & Falsafi, S. R. (2023). Ovalbumin, an outstanding food hydrocolloid: Applications, technofunctional attributes, and nutritional facts, A systematic review. Food Hydrocolloids, 139, 108514. https://doi.org/10.1016/j.foodhyd.2023.108514
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Ito, K., Seri, A., Kimura, F., & Matsudomi, N. (2007). Site-specific Glycosylation at Asn-292 in Ovalbumin is Essential to Efficient Secretion in Yeast. The Journal of Biochemistry, 141(2), 193–199. https://doi.org/10.1093/jb/mvm021
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Rupa, P., & Mine, Y. (2003). Immunological comparison of native and recombinant egg allergen, ovalbumin, expressed inEscherichia coli. Biotechnology Letters, 25(22), 1917–1924. https://doi.org/10.1023/b:bile.0000003987.60659.ea
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Upadhyay, V., Singh, A., & Panda, A. K. (2016). Purification of recombinant ovalbumin from inclusion bodies of Escherichia coli. Protein Expression and Purification, 117, 52–58. https://doi.org/10.1016/j.pep.2015.09.015
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