A Pichia pastoris-based platform for large-scale production of functional recombinant human serum albumin with therapeutic efficacy

B-017 A Purified Recombinant Human Albumin Produced in Thermothelomyces heterothallica (C1) Better Mimics Native Human Serum Albumin than Recombinant Albumin from Other Expression Systems

Recombinant human albumin (rHA) is widely used as an alternative to plasma-derived human serum albumin (HSA) in diagnostic and bioanalytical applications. However, rHA produced in different expression systems can exhibit varying post-translational modifications (PTMs), impurity profiles, and free thiol content, w...

Ogataea Yeast Platform for Recombinant Porcine Interferon-Alpha 1 Production: Toward Alternative Biotherapeutics for Swine Health Management

Infectious diseases in swine demand affordable, broad-spectrum antiviral strategies, such as recombinant interferons (IFNs). However, commercial yeast expression platforms often present financial barriers through licensing royalties. To provide a cost-effective regional alternative, we evaluated the domestic, thermotol...

Preperation of an engineered tryptophan-depleted protein in Pichia pastoris and evaluation of its dietary anti-tumor efficacy.

B-168 Purified Recombinant Human Albumin Produced in Thermothelomyces heterothallica (C1) Demonstrates Effective Blocking and Comparable Surface Binding to Other Recombinant and Native Albumins

Recombinant and native human serum albumins (rHA and HSA) are widely used as blocking agents to prevent nonspecific binding of enzymes, antibodies, and other biomolecules to surfaces. HSA is primarily used in diagnostic assays to reduce background signals and improve assay sensitivity, though assay performance ca...

Efficient production of recombinant human serum albumin in Escherichia coli via oxidative folding mediated by the a domain of protein disulfide isomerase.

It is demonstrated that PDI(a)-mediated cis-fusion enables high-yield production of structurally native-like and functionally competent HSA in the bacterial cytosol and provides a practical platform for producing complex disulfide-rich proteins in E. coli.

Harnessing Yarrowia lipolytica as a platform for animal-free and secretory production of human lactoferrin.

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.