Investigation of protein expression profiles of erythritol-producing Candida magnoliae in response to glucose perturbation

Hyo Jin Kim, Hyeong Rho Lee, Chang Sup Kim, Yong Su Jin, Jin Ho Seo

Research output: Contribution to journalArticlepeer-review


Protein expression patterns of an erythritol-producing yeast, Candida magnoliae, were analyzed to identify differentially expressed proteins in response to glucose perturbation. Specifically, wild type C. magnoliae was grown under high and low glucose conditions and the cells were harvested at both mid-exponential and erythritol production phases for proteomic studies. In order to analyze intracellular protein abundances from the harvested cells quantitatively, total intracellular proteins were extracted and applied to two-dimensional gel electrophoresis for separation and visualization of individual proteins. Among the proteins distributed in the range of pI 4-7 and molecular weight 29-97. kDa, five osmo-responsive proteins were drastically changed in response to glucose perturbation. Hsp60 (Heat-shock protein 60), transaldolase and NADH:quinone oxidoreductase were down-regulated under the high glucose condition and Bro1 (BCK1-like Resistance to Osmotic shock) and Eno1 (enolase1) were up-regulated. These proteins are directly or indirectly related with cellular stress response. Importantly, protein expression patterns of Hsp60, Bro1 and Eno1 were strongly correlated with previous studies identifying the proteins perturbed by osmotic stress for other organisms including Saccharomyces cerevisiae.

Original languageEnglish (US)
Pages (from-to)174-180
Number of pages7
JournalEnzyme and Microbial Technology
Issue number3
StatePublished - Aug 15 2013


  • Candida magnoliae
  • Erythritol
  • Osmo-responsive protein
  • Proteomics

ASJC Scopus subject areas

  • Biochemistry
  • Biotechnology
  • Applied Microbiology and Biotechnology


Dive into the research topics of 'Investigation of protein expression profiles of erythritol-producing Candida magnoliae in response to glucose perturbation'. Together they form a unique fingerprint.

Cite this