Biotechnology Letters

, Volume 18, Issue 10, pp 1223–1228

Secretion of heterologous cyclodextrin glycosyltransferase of Bacillus sp. E1 from Escherichia coli

  • Jeongsik Yong
  • Jin Nam Choi
  • Sung Soon Park
  • Cheon Seok Park
  • Kwan Hwa Park
  • Yang Do Choi
Article

DOI: 10.1007/BF00128597

Cite this article as:
Yong, J., Choi, J.N., Park, S.S. et al. Biotechnol Lett (1996) 18: 1223. doi:10.1007/BF00128597

Summary

To characterize the molecular properties of CGTase from alkalophilic Bacillus sp. E1 (BCGTE1), a genomic clone for a CGTase was isolated. Expression of recombinant BCGTE1 in E. coli was analyzed by immunoblotting. It showed that the nascent recombinant BCGTE1 expressed was 87 kDa but it was processed into the mature enzyme of 81 kDa. With the process it was secreted predominantly into the culture medium via periplasmic space. This feature is different from other Bacillus CGTases expressed in E. coli, which were present mostly in the periplasmic space.

Copyright information

© Chapman & Hall 1996

Authors and Affiliations

  • Jeongsik Yong
    • 1
    • 2
  • Jin Nam Choi
    • 1
    • 2
  • Sung Soon Park
    • 1
    • 2
  • Cheon Seok Park
    • 1
    • 3
  • Kwan Hwa Park
    • 1
    • 3
  • Yang Do Choi
    • 1
    • 2
  1. 1.Research Center for New Bio-Materials in Agriculture, Seoul National UniversitySuwonKorea
  2. 2.Department of Agricultural ChemistrySeoul National UniversitySuwonKorea
  3. 3.Department of Food Science and TechnologySeoul National UniversitySuwonKorea