Purification and characterisation of an alkaline protease used in tannery industry from Bacillus licheniformis

Biotechnol Lett. 2004 Sep;26(18):1421-4. doi: 10.1023/B:BILE.0000045642.19299.3f.

Abstract

An extracellular alkaline protease produced by Bacillus licheniformis AP-1 was purified 76-fold, yielding a single 28 kDa band on SDS-PAGE. It was optimally active at pH 11 and at 60 degrees C (assayed over 10 min). The protease was completely inhibited by phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca2+ and Mg2+ addition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / classification
  • Bacillus / enzymology*
  • Enzyme Activation
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Industry
  • Molecular Weight
  • Serine Endopeptidases / analysis
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / isolation & purification*
  • Species Specificity
  • Temperature

Substances

  • Serine Endopeptidases
  • microbial serine proteinases