Mechanistic Modeling of Size Exclusion Chromatography-Assisted In Vitro Refolding of the Recombinant Biosimilar Teriparatide (PTH-34).

ABSTRACT: In vitro protein refolding is one of the critical unit operations in manufacturing recombinant peptides expressed using Escherichia coli as host cells. This study is focused on designing size exclusion chromatography-assisted in vitro refolding process for biosimilar recombinant parathyroid hormone. Inclusion bodies (IBs) of recombinant parathyroid hormone were solubilized at higher pH, and in vitro refolding was performed using size exclusion chromatography. In the first part of the investigation, DoE-based empirical optimization was performed to achieve a higher refolding yield for a biosimilar recombinant parathyroid hormone. The effect of solubilized inclusion body (IB) feed volume, concentration of IBs, and residence time on in vitro refolding of rec

SUBMITTER: Ughade S 

PROVIDER: S-EPMC10809233 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature