Screening, purification and characterization of a novel cold-active and organic solvent-tolerant lipase from Stenotrophomonas maltophilia CGMCC 4254

Bioresour Technol. 2013 Nov:148:114-20. doi: 10.1016/j.biortech.2013.08.101. Epub 2013 Aug 27.

Abstract

An extracellular organic solvent-tolerant and cold-active lipase producing bacterium was isolated from oil-contaminated soil samples, and identified taxonomically as Stenotrophomonas maltophilia. The lipase from S. maltophilia CGMCC 4254 (SML) was purified 60.5-fold to homogeneity with 38.9 U/mg specific activity. Partially purified SML displayed remarkable stability in 50% and 100% (v/v) hydrophobic organic solvents after incubation for 7 days. The enzyme also retained more than 50% of its residual activity in several pure hydrophilic organic solvents after incubation for 7 days. SML showed 57% maximum activity at 5°C, and had optimal activity at 35°C. These unique properties of SML make it promising as a biocatalyst for industrial processes.

Keywords: Cold-active; Lipase; Non-aqueous; Solvent tolerant; Stenotrophomonas maltophilia.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cold Temperature*
  • Enzyme Stability / drug effects
  • Hydrogen-Ion Concentration / drug effects
  • Lipase / biosynthesis
  • Lipase / isolation & purification*
  • Lipase / metabolism*
  • Organic Chemicals / pharmacology*
  • Phylogeny
  • Solvents / pharmacology*
  • Stenotrophomonas maltophilia / drug effects
  • Stenotrophomonas maltophilia / enzymology*
  • Substrate Specificity / drug effects

Substances

  • Organic Chemicals
  • Solvents
  • Lipase