High-level production of Fc-fused kringle domain in Pichia pastoris

J Ind Microbiol Biotechnol. 2014 Jun;41(6):989-96. doi: 10.1007/s10295-014-1435-2. Epub 2014 Mar 30.

Abstract

Recently, as a new non-immunoglobulin-based protein scaffold, a human kringle domain was successfully engineered toward biologically functional agonists and antagonists. In this study, the fed-batch cultivation conditions were optimized for enhanced production of an Fc-fused kringle domain (KD548-Fc) in Pichia pastoris. Fed-batch cultivations were performed in 5-l laboratory-scale bioreactors, and in order to find the optimal conditions for high-level production of KD548-Fc, several parameters including the initial carbon source (glycerol) concentration, temperature, and pH were investigated. When cells were cultivated at pH 4.0 and 25 °C with 9.5 % glycerol in the initial medium, the highest production yield (635 mg/l) was achieved with high productivity (7.2 mg/l/h). Furthermore, functional KD548-Fc was successfully purified from the culture broth using a simple purification procedure with high purity and recovery yield.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bioreactors
  • Culture Media
  • Fermentation
  • Glycerol / metabolism
  • Humans
  • Hydrogen-Ion Concentration
  • Immunoglobulin Fc Fragments / genetics
  • Kringles / genetics*
  • Pichia / genetics*
  • Pichia / growth & development
  • Pichia / metabolism
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / isolation & purification
  • Temperature

Substances

  • Culture Media
  • Immunoglobulin Fc Fragments
  • Recombinant Fusion Proteins
  • Glycerol