Jul 2026· Bioprocess and biosystems engineering (Print)· Vol 49, pp. 2225 - 2237· 0 citations· 40 references
Medicine
TL;DR
A refolding-free bioprocess for high-yield soluble expression of B2036 in E. coli using SUMO fusion provides a valuable reference for developing efficient soluble expression and downstream purification processes of other intrachain disulfide-bonded proteins in E. coli.
Protein L is a κ light-chain-binding protein, which is widely used as an affinity ligand for antibody purification and characterization. However, manufacturable recombinant Protein L ligands remain insufficiently studied, particularly regarding how domain architecture affects production, processability, and product qua...
Xiao-Yong Jiang, Rui-Rui Wu, Ke-Xin Xu et al.· Protein Expression and Purif...· 0 citations
It is demonstrated that maximizing recombinant protein production requires optimization of both yield and structural quality and establish complementary strategies for improving secreted protein expression in Pichia.
A case-study evaluation of a pBR322-derived expression system, previously applied to therapeutic peptides and insulin analogs, in combination with fed-batch cultivation for recombinant production of methionine aminopeptidase in E. coli, evaluating the performance of this system for methionine aminopeptidase as a stress...
G. Kuznetsov, Marina Yarovikova, E. Buslaeva et al.· Protein Expression and Purif...· 0 citations
The highest yield, most uniform, and thermally stable anti-hCD45 NB preparation was obtained with signal-peptide-mediated periplasmic targeting and flow cytometry confirmed functional binding of all tested anti-hCD45 NB to CD45-positive Jurkat cells.
J. Meyer, Marie Beneke, Sadija Altmüller et al.· Microbial Cell Factories· 0 citations
The first peptide affinity ligands targeting the baculoviral envelope glycoprotein GP64 for the purification of active Baculovirus particles are introduced, establishing SB4-POROS as a promising technology with a favorable projected cost structure for Baculovirus purification.
Will Smith, S. Sripada, Yuxuan Wu et al.· Journal of Chromatography A· 0 citations
Y. lipolytica is developed as a microbial platform for high-level production and secretion of recombinant hLF and established as a promising platform for sustainable, animal-free manufacturing of lactoferrin and potentially other high-value nutritional and therapeutic proteins.
Zi-Zhao Wu, Hong-Chao Ren, Pei-Yan Cai et al.· Bioresource Technology· 0 citations
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