World Journal of Microbiology and Biotechnology

, Volume 24, Issue 2, pp 237–243

Biosynthesis and properties of an extracellular thermostable serine alkaline protease from Virgibacillus pantothenticus

Original Paper

DOI: 10.1007/s11274-007-9462-z

Cite this article as:
Gupta, A., Joseph, B., Mani, A. et al. World J Microbiol Biotechnol (2008) 24: 237. doi:10.1007/s11274-007-9462-z


In this communication, we report the presence of a newly identified serine alkaline protease producing bacteria, Virgibacillus pantothenticus (MTCC 6729) in the fresh chicken meat samples and the factors affecting biosynthesis as well as characterization of protease. The strain produced only 14.3 U ml−1 protease in the standard medium after 72 h of incubation, while in optimized culture conditions the production of protease was increased up to 18.2 U ml−1. The strain was able to produce protease at 40°C at pH 9.0. The addition of dextrose and casein improved protease production. The protease was partially purified and characterized in terms of pH and temperature stability, effect of metal ions and inhibitors. The protease was found to be thermostable alkaline by retaining its 100% and 85% stability at pH 10.0 and at 50°C respectively. The protease was compatible with some of the commercial detergents tested, and was effective in removing protein stains from cotton fabrics. The V. pantothenticus, MTCC 6729 protease appears to be potentially useful as an additive in detergents as a stain remover and other bio-formulations.


Alkaline protease Detergent compatibility Enzyme Serine protease Virgibacilluspantothenticus 

Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Amit Gupta
    • 1
  • Babu Joseph
    • 2
  • Abin Mani
    • 2
  • George Thomas
    • 2
  1. 1.National Institute of Pharmaceutical Education and ResearchChandigarhIndia
  2. 2.College of Biotechnology and Allied SciencesAllahabad Agricultural Institute - Deemed UniversityAllahabadIndia

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