Abstract
We have developed a recombinant expression system to produce a series of novel recombinant human gelatins that can substitute for animal sourced gelatin preparations currently used in pharmaceutical and nutraceutical applications. This system allows the production of human sequence gelatins, or, if desired, gelatins from any other species depending on the availability of the cloned gene. The gelatins produced with this recombinant system are of defined molecular weight, unlike the animal-sourced gelatins, which consist of numerous polypeptides of varying size. The fermentation and purification process used to prepare these recombinant gelatins does not use any human- or animal-derived components and thus this recombinant material should be free from viruses and agents that cause transmissible spongiform encephalopathies. The recombinant gelatins exhibit lot-to-lot reproducibility and we have performed extensive analytical testing on them. We have demonstrated the utility of these novel gelatins as biological stabilizers and plasma expanders, and we have shown they possess qualities that are important in applications where gel formation is critical. Finally, we provide examples of how our system allows the engineering of these recombinant gelatins to optimize the production process.
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Acknowledgements
The authors would like to thank Elaine Lee for preparation of this manuscript. Table 2 is reprinted from Advanced Drug Delivery Reviews 55:1547–1567, 2003; Olsen D. et al., Recombinant Collagen and Gelatin for Drug Delivery with permission from Elsevier.
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Olsen, D., Chang, R., Williams, K.E., Polarek, J.W. (2008). The Development of Novel Recombinant Human Gelatins as Replacements for Animal-Derived Gelatin in Pharmaceutical Applications. In: Pasupuleti, V., Demain, A. (eds) Protein Hydrolysates in Biotechnology. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6674-0_12
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DOI: https://doi.org/10.1007/978-1-4020-6674-0_12
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