Jul 2026· Bioprocess and biosystems engineering (Print)· Vol 49, pp. 2213 - 2223· 0 citations· 36 references
Medicine
TL;DR
This study provides the first in vivo evidence confirming the therapeutic equivalence and dose-effect relationship of P. pastoris-derived rHSA compared with pHSA, supporting its potential as a viable clinical substitute for plasma-derived albumin.
It is demonstrated that rHA produced in Thermothelomyces heterothallica (C1) more closely mimics native HSA than recombinant albumins produced in yeast and plant expression systems.
Audrianna Kern, Garry Smith, A. Okerlund et al.· Clinical Chemistry· 0 citations
Based on the proof-of-concept results in this study, the OP39 platform can be further developed into a viable, full freedom-to-operate system for local or regional biomanufacturing of biologically active veterinary therapeutics to support livestock health management.
Benjamas Liwnaree, Thorntun Deangphare, C. Assana et al.· Microorganisms· 0 citations
A novel tryptophan-depleted protein (TDP) is developed through protein engineering combined with the Pichia pastoris expression system, for dietary intervention to suppress tumor growth in vivo and establishes a novel strategic framework for dietary intervention in adjuvant cancer therapy.
Huijia Dai, Yuluo Chen, Ya-Ying Xie et al.· Sheng wu gong cheng xue bao...· 0 citations
Findings support C1-derived rHA as a reliable alternative for surface blocking and coating applications, offering comparable performance while reducing variability and production cost limitations associated with existing albumin products.
Audrianna Kern, A. Okerlund, C. Kunkler et al.· Clinical Chemistry· 0 citations
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.
R. Urade, Yuki Yamaguchi, K. Morishima et al.· Journal of Bioscience and Bi...· 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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