Production of a Recombinant Non-Hydroxylated Gelatin Mimetic in Pichia pastoris for Biomedical Applications

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dc.identifier.uri http://dx.doi.org/10.15488/9297
dc.identifier.uri https://www.repo.uni-hannover.de/handle/123456789/9350
dc.contributor.author Gellermann, Pia
dc.contributor.author Schneider-Barthold, Caroline
dc.contributor.author Bolten, Svenja Nic
dc.contributor.author Overfelt, Ethan
dc.contributor.author Scheper, Thomas
dc.contributor.author Pepelanova, Iliyana
dc.date.accessioned 2020-01-31T09:28:10Z
dc.date.available 2020-01-31T09:28:10Z
dc.date.issued 2019
dc.identifier.citation Gellermann, P.; Schneider-Barthold, C.; Bolten, S.N.; Overfelt, E.; Scheper, T. et al.: Production of a Recombinant Non-Hydroxylated Gelatin Mimetic in Pichia pastoris for Biomedical Applications. In: Journal of Functional Biomaterials 10 (2019), Nr. 3, 39. DOI: https://doi.org/10.3390/jfb10030039
dc.description.abstract Proteins derived from the natural extracellular matrix like collagen or gelatin are common in clinical research, where they are prized for their biocompatibility and bioactivity. Cells are able to adhere, grow and remodel scaffolds based on these materials. Usually, collagen and gelatin are sourced from animal material, risking pathogenic transmission and inconsistent batch-to-batch product quality. A recombinant production in yeast circumvents these disadvantages by ensuring production with a reproducible quality in animal-component-free media. A gelatin mimetic protein, based on the alpha chain of human collagen I, was cloned in Pichia pastoris under the control of the methanol-inducible alcohol oxidase (AOX1) promoter. A producing clone was selected and cultivated at the 30 L scale. The protein was secreted into the cultivation medium and the final yield was 3.4 g·L−1. Purification of the target was performed directly from the cell-free medium by size exclusion chromatography. The gelatin mimetic protein was tested in cell culture for biocompatibility and for promoting cell adhesion. It supported cell growth and its performance was indistinguishable from animal-derived gelatin. The gelatin-mimetic protein represents a swift strategy to produce recombinant and human-based extracellular matrix proteins for various biomedical applications. eng
dc.language.iso eng
dc.publisher Basel : MDPI AG
dc.relation.ispartofseries Journal of Functional Biomaterials 10 (2019), Nr. 3
dc.rights CC BY 4.0 Unported
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject Gelatin-mimetic protein eng
dc.subject Komagataella pfaffi (Pichia pastoris) eng
dc.subject Recombinant ECM-protein eng
dc.subject Recombinant gelatin eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.title Production of a Recombinant Non-Hydroxylated Gelatin Mimetic in Pichia pastoris for Biomedical Applications
dc.type article
dc.type Text
dc.relation.issn 2079-4983
dc.relation.doi https://doi.org/10.3390/jfb10030039
dc.bibliographicCitation.issue 3
dc.bibliographicCitation.volume 10
dc.bibliographicCitation.firstPage 39
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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