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Information for

C. Perry Chou

Canada Research Chair in Biomanufacturing & Editor of Biotechnology Advances & Professor

C. Perry ChouDegrees

  • BSc, National Taiwan University
  • MSc, National Taiwan University
  • PhD, Rice University

Research interests

  • Biochemical engineering
  • Molecular biology
  • Microbial biotechnology
  • Genetic engineering
  • Metabolic engineering
  • Protein engineering

My major research interests include recombinant protein production, biofuel production, and bioprocessing technology. I have applied biological sciences and engineering theories to develop novel and effective bioprocesses for the production of recombinant proteins (including industrial enzymes and therapeutic proteins) and metabolites (including biohydrogen, biodiesel, and biobutanol). Such bioprocess development includes upstream technology for biological strain construction, midstream technology for bioreaction (i.e., cultivation), and downstream processing for bioproduct recovery and purification.

Background

Recombinant Deoxyribonucleic Acid (DNA) technology is a bio-tool developed in 1970 and plays a pivot role in today's biosciences and bioengineering. Its application presents tremendous impacts in biochemical, biomedical, pharmaceutical, agricultural, food, and environmental industries. While acting as a novel tool for unraveling scientific mysteries, it also provides an efficient means to produce desired proteins in large amounts. In addition, it can be adopted  for genetic manipulation of microbial strains to obtain desired traits for enhancing biomanufacturing.

Brief Research Description

Our strategies for enhancing biomanufacturing are mainly focused on developing effective microbial host/vector systems using recombinant DNA technology. Several industrial enzymes (e.g., penicillin acylases and lipases), therapeutic proteins (e.g., human CD83), reporter proteins, metabolites (e.g. biohydrogen, biodiesel, and biobutanol) are used as target products for various biotechnological explorations, including: identification of expression limiting steps, protein secretion (i.e., periplasmic or extracellular expression), surface display, posttranslational issues, physiological manipulation of host strains, in-vivo protein misfolding (i.e., soluble expression), in-vitro protein refolding, fusion-protein technology, molecular manipulation of proteins, pathway knockouts, pathway constructions, etc.

Selected references

  • Narayanan N, Chou CP (2009) Alleviation of proteolytic sensitivity to enhance recombinant lipase production in Escherichia coli. Appl. Environ. Microbiol. 75:5424-5427.
  • Xu Y, Zhang L, Yao W, Yedahalli SS, Brand S, Moo-Young M, Chou CP (2009) Bioprocess development for production, purification, and structural characterization of recombinant hCD83ext as a potential therapeutic protein. Protein Express. Purif. 65:92-99.
  • Xu Y, Yasin A, Tang R, Scharer JM, Moo-Young M, Chou CP (2008) Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation. Appl. Microbiol. Biotechnol. 81:79-87.
  • Chou CP (2007) Engineering cell physiology to enhance recombinant protein production in Escherichia coli. Appl. Microbiol. Biotechnol. 76:521-532.
  • Wu MS, Pan KL, Chou CP (2007) Effect of heat-shock proteins for relieving physiological stress and enhancing the production of penicillin acylase in Escherichia coli. Biotechnol. Bioeng. 96:956-966.
  • Narayanan N, Hsieh M-Y, Xu Y, Chou CP (2006) Arabinose-induction of lac-derived promoter systems for penicillin acylase production in Escherichia coli. Biotechnol. Prog. 22:617-625.
  • Xu Y, Weng C-L, Narayanan N, Hsieh M-Y, Anderson WA, Scharer JM, Moo-Young M, Chou CP (2005) Chaperone-mediated folding and maturation of penicillin acylase precursor in the cytoplasm of Escherichia coli. Appl. Environ. Microbiol. 71:6247-6253.
  • Pan K-L, Hsiao H-C, Weng C-L, Wu M-S, Chou CP (2003) Roles of DegP in prevention of protein misfolding in the periplasm upon overexpression of penicillin acylase in Escherichia coli. J. Bacteriol. 185:3020-3030.
  • Lin W-J, Huang S-W, Chou CP (2001) DegP coexpression minimizes inclusion body formation upon overproduction of recombinant penicillin acylase in Escherichia coli. Biotechnol. Bioeng. 73:484-492.
  • Chou CP, Yu C-C, Tseng J-H, Lin M-I, Lin H-K (1999)  Genetic manipulation to identify limiting steps and develop strategies for high-level expression of penicillin acylase in Escherichia coli. Biotechnol. Bioeng. 63:263-272.
Affiliation: 
University of Waterloo