Effect of the C-terminal domains and terminal residues of catalytic domain on enzymatic activity and thermostability of lichenase from Clostridium thermocellum

Biotechnol Lett. 2010 Jul;32(7):963-7. doi: 10.1007/s10529-010-0241-9. Epub 2010 Mar 13.

Abstract

To elucidate the effects of C-terminal domains of LicMB (mature lichenase from Clostridium thermocellum) and terminal residues of LicMB-CD (catalytic domain of LicMB) on the properties of lichenase, a series of truncated genes were constructed and expressed in E. coli. The Thr-Pro box had a positive effect while the dockerin domain had a negative impact on the properties of LicMB. The N-terminal 10-25th and C-terminal 1-9th residues of LicMB-CD were necessary to retain high thermostability while the N-terminal 1-7th and C-terminal 1-3rd residues were not necessary to maintain enzymatic activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Catalytic Domain
  • Clostridium thermocellum / enzymology*
  • Enzyme Stability
  • Escherichia coli / genetics
  • Gene Expression
  • Glycoside Hydrolases / chemistry*
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism*
  • Mutant Proteins / chemistry
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism
  • Protein Stability
  • Sequence Deletion
  • Temperature

Substances

  • Bacterial Proteins
  • Mutant Proteins
  • Glycoside Hydrolases
  • licheninase