| Protein name |
Alpha-casein |
| Host compatibility |
Escherichia coli |
| Yield |
1.13 g/L (Y. Wang et al., 2020)
|
| Scale (in specific example) |
Lab scale in bioreactor (Y. Wang et al., 2020)
|
| Biggest scale product has been develloped in this organism |
Lab scale in bioreactor (Y. Wang et al., 2020)
|
| Regulatory status in Europe |
Not allowed |
| Regulatory status in other parts of the world |
No FDA GRAS approval in US, not allowed in Canada |
| Companies producing this protein in this organism |
NA |
| Extra/remark |
Casein molecules (alpha, beta and kappa) are assembled into supramolecular protein structures called casein micelles. These micelles are destabilized during cheese making, which results into the aggregation of the casein proteins into a protein network. All three types of casein proteins are thus needed together (Hettinga & Bijl, 2022).
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| Publications/references |
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Wang, Y., Kubiczek, D., Horlamus, F., Raber, H. F., Hennecke, T., Einfalt, D., Henkel, M., Hausmann, R., Wittgens, A., & Rosenau, F. (2020). Bioconversion of lignocellulosic ‘waste’ to high‐value food proteins: Recombinant production of bovine and human αS1‐casein based on wheat straw lignocellulose. GCB Bioenergy, 13(4), 640–655. https://doi.org/10.1111/gcbb.12791
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Broyard, C., & Gaucheron, F. (2015). Modifications of structures and functions of caseins: a scientific and technological challenge. Dairy Science and Technology, 95(6), 831–862. https://doi.org/10.1007/s13594-015-0220-y
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Chezan, D., Fuhrmann, P. L., Bender, D., Rennhofer, H., Domig, K. J., & Dewi, B. P. (2025). Physicochemical properties of native and precision fermentation-derived bovine β-casein: structural and functional insights. Food Hydrocolloids, 171, 111797. https://doi.org/10.1016/j.foodhyd.2025.111797
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Knychala, M. M., Boing, L. A., Ienczak, J. L., Trichez, D., & Stambuk, B. U. (2024). Precision Fermentation as an Alternative to Animal Protein, a Review. Fermentation, 10(6), 315. https://doi.org/10.3390/fermentation10060315
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Hettinga, K., & Bijl, E. (2022). Can recombinant milk proteins replace those produced by animals? Current Opinion in Biotechnology, 75, 102690. https://doi.org/10.1016/j.copbio.2022.102690
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Lanquar, V., El-Richani, M., Hathwaik, L., & Klemaszewski, J. (2024, September 3). US20240102072A1 - Food compositions comprising recombinant milk proteins. Retrieved September 1, 2025, from https://patents.google.com/patent/US20240102072A1
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Hochwallner, H., Schulmeister, U., Swoboda, I., Spitzauer, S., & Valenta, R. (2014). Cow’s milk allergy: From allergens to new forms of diagnosis, therapy and prevention. Methods, 66(1), 22–33. https://doi.org/10.1016/j.ymeth.2013.08.005
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