Purification and properties of an endo-1,4-beta-glucanase translated from a Clostridium josui gene in Escherichia coli

Appl Environ Microbiol. 1990 Apr;56(4):1175-8. doi: 10.1128/aem.56.4.1175-1178.1990.

Abstract

An endoglucanase encoded by a gene of Clostridium josui was expressed in Escherichia coli and purified. The homogeneous enzyme, with a molecular weight of 39,000, revealed maximum endoglucanase activity at pH 7.2 to 7.5 and a temperature of 65 to 70 degrees C. The enzyme was stable at a temperature lower than 45 degrees C (the growth temperature of the bacterium) in the range of pH 4.5 to 9.0. The amino acid sequence of the enzyme at the N terminus was Val-Glu-Glu-Asp-Ser-Ser-His-Leu-Ile-Thr-Asn-Gln-Ala-Lys-Lys----. The enzyme hydrolyzed cellotetraose to cellobiose and then transferred cellobiose to the residual cellotetraose. The resulting cellohexaose was cleaved to cellotriose.

MeSH terms

  • Amino Acid Sequence
  • Cellobiose
  • Cellulase / genetics*
  • Cellulase / isolation & purification
  • Cellulase / metabolism
  • Cellulose* / analogs & derivatives*
  • Clostridium / enzymology*
  • Clostridium / genetics
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Genes, Bacterial
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Molecular Weight
  • Oligosaccharides
  • Protein Biosynthesis
  • Substrate Specificity
  • Temperature
  • Tetroses*
  • Transformation, Genetic

Substances

  • Oligosaccharides
  • Tetroses
  • Cellobiose
  • cellotetraose
  • Cellulose
  • Cellulase