Biotechnology Letters

, Volume 27, Issue 16, pp 1195–1198

Purification and Characterization of an Extracellular Cold-Active Serine Protease from the Psychrophilic Bacterium Colwellia sp. NJ341

  • Quan-Fu Wang
  • Jin-Lai Miao
  • Yan-Hua Hou
  • Yu Ding
  • Guo-Dong Wang
  • Guang-You Li
Article

DOI: 10.1007/s10529-005-0016-x

Cite this article as:
Wang, Q., Miao, J., Hou, Y. et al. Biotechnol Lett (2005) 27: 1195. doi:10.1007/s10529-005-0016-x

Abstract

Colwellia sp. NJ341, isolated from Antarctic sea ice, secreted a cold-active serine protease. The purified protease had an apparent Mr of 60 kDa by SDS-PAGE and MALDI-TOF MS. It was active from pH 5–12 with maximum activity at 35 °C (assayed over 10 min). Activity at 0 °C was nearly 30% of the maximum activity. It was completely inhibited by phenylmethylsulfonyl fluoride.

Keywords

Antarcticcold-active serine proteaseColwelliapsychrophilic bacteria

Copyright information

© Springer 2005

Authors and Affiliations

  • Quan-Fu Wang
    • 1
    • 2
  • Jin-Lai Miao
    • 2
  • Yan-Hua Hou
    • 3
  • Yu Ding
    • 2
  • Guo-Dong Wang
    • 2
  • Guang-You Li
    • 2
  1. 1.College of life SciencesOcean University of ChinaQingdaoP.R. China
  2. 2.Key Laboratory of Marine Bio-active Substances, First Institute of OceanorgarphyState Oceanic AdministrationQingdaoP.R. China
  3. 3.Harbin Institute of TechnologyWeihaiP.R. China