Characterization of a thermostable alkaline protease produced by marine Streptomyces fungicidicus MML1614

Bioprocess Biosyst Eng. 2009 Oct;32(6):791-800. doi: 10.1007/s00449-009-0305-1. Epub 2009 Feb 22.

Abstract

Totally 191 different marine actinomycetes were isolated from 256 different marine samples collected from the Bay of Bengal and its associated Pulicat lake and Pichavaram mangrove, India. Among them, 157 produced caseinase, 113 produced gelatinase and 108 produced both the protease enzymes. An isolate coded as MML1614 was selected for further study as it exhibited high proteolytic activity. The MML1614 was identified as Streptomyces fungicidicus based on polyphasic taxonomical approach including 16S rRNA sequence analysis. The culture conditions were standardized for the growth and protease production in S. fungicidicus MML1614. The protease was isolated from a 6-day-old culture filtrate of S. fungicidicus MML1614 and partially purified up to 4.5-fold. The protease was optimally active at pH 9 and 40 degrees C and it was stable up to pH 11 and 60 degrees C. PMSF and NaCl inhibited the enzyme activity up to 22 and 11%, respectively. The partially purified protease removed the blood stain more effectively when combined with different detergents than the detergents alone.

MeSH terms

  • Chelating Agents / pharmacology
  • Culture Media
  • Detergents
  • Enzyme Stability
  • Fresh Water / microbiology
  • Hydrogen-Ion Concentration
  • India
  • Kinetics
  • Laundering
  • Metals / pharmacology
  • Protease Inhibitors / pharmacology
  • Serine Endopeptidases / biosynthesis
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / metabolism*
  • Streptomyces / classification
  • Streptomyces / enzymology*
  • Streptomyces / genetics
  • Streptomyces / isolation & purification
  • Temperature

Substances

  • Chelating Agents
  • Culture Media
  • Detergents
  • Metals
  • Protease Inhibitors
  • Serine Endopeptidases
  • microbial serine proteinases