Related Experiment Video
Updated: Apr 12, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Cold adaptation of a psychrophilic chaperonin from Psychrobacter sp. and its application for heterologous protein
Han-Woo Kim1, Ah Ram Wi, Byoung Wook Jeon
1Division of Polar Life Sciences, Korea Polar Research Institute (KOPRI), 26, Songdomirae-ro, Yeonsu-gu, Incheon, 406-840, Republic of Korea, hwkim@kopri.re.kr.
Objectives:
A chaperonin, PsyGroELS, from the Antarctic psychrophilic bacterium Psychrobacter sp. PAMC21119, was examined for its role in cold adaptation when expressed in a mesophilic Escherichia coli strain.
Results:
Growth of E. coli harboring PsyGroELS at 10 °C was increased compared to the control strain. A co-expression system using PsyGroELS was developed to increase productivity of the psychrophilic enzyme PsyEst9. PsyEst9 was cloned and expressed using three E. coli variants that co-expressed GroELS from PAMC21119, E. coli, or Oleispira antarctica RB8(T). Co-expression with PsyGroELS was more effective for the production of PsyEst9 compared tothe other chaperonins.
Conclusion:
PsyGroELS confers cold tolerance to E. coli, and shows potential as an effective co-expression system for the stable production of psychrophilic proteins.
More Related Videos
Related Concept Videos
Factors Influencing Microbial Growth: Temperature
Bacterial Protein Maturation
Other Stress Responses in Bacteria
Diversity of Archaea IV
Diversity of Archaea III
Molecular Chaperones and Protein Folding
The...

