Molecular cloning and sequence analysis of an extracellular protease from four Bacillus subtilis strains

Biosci Biotechnol Biochem. 2013;77(4):870-3. doi: 10.1271/bbb.120920. Epub 2013 Apr 7.

Abstract

Four Bacillus subtilis strains were isolated from traditional fermented foods, and the sequences of their extracellular alkaline proteases (AprE) were analyzed and cloned. The recombinant enzymes synthesized by means of Escherichia coli exhibited high proteolytic activity. AprE CN2 showed hydrolytic activity 4-fold higher than that of AprE 168. This activity was also seen in the presence of relatively high NaCl concentrations.

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / cytology
  • Bacillus subtilis / enzymology*
  • Bacillus subtilis / genetics*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Cloning, Molecular
  • Endopeptidases / chemistry
  • Endopeptidases / genetics*
  • Endopeptidases / metabolism
  • Extracellular Space / enzymology*
  • Kinetics
  • Molecular Sequence Data
  • Sequence Analysis*
  • Sodium Chloride / pharmacology

Substances

  • Bacterial Proteins
  • Sodium Chloride
  • Endopeptidases
  • alkaline protease