Production, partial purification and characterization of organic solvent tolerant lipase from Burkholderia multivorans V2 and its application for ester synthesis

Bioresour Technol. 2009 Jul;100(13):3374-81. doi: 10.1016/j.biortech.2009.02.011. Epub 2009 Mar 12.

Abstract

Burkholderia multivorans V2 (BMV2) isolated from soil was found to produce an extracellular solvent tolerant lipase (6.477 U/mL). This lipase exhibited maximum stability in n-hexane retaining about 97.8% activity for 24h. After performing statistical optimization of medium components for lipase production, a 2.2-fold (14 U/mL) enhancement in the lipase production was observed. The crude lipase from BMV2 was partially purified by ultrafiltration and gel permeation chromatography with 24.64-fold purification. The K(m) and V(max) values for partially purified BMV2 lipase were found to be 1.56 mM and 5.62 micromoles/mg min. The metal ions Ca(2+), Mg(2+) and Mn(2+) had stimulatory effect on lipase activity, whereas Cu(2+), Fe(2+) and Zn(2+) strongly inhibited the lipase activity. EDTA and PMSF at 10mM concentration strongly inhibited the lipase activity. Non-ionic and anionic surfactants stimulated the lipase activity. BMV2 lipase was proved to be efficient in synthesis of ethyl butyrate ester under non-aqueous environment.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biotechnology / methods*
  • Burkholderia / enzymology*
  • Butyrates / chemistry
  • Carbon / chemistry
  • Chemistry, Organic / methods
  • Chromatography / methods
  • Esters / chemical synthesis*
  • Esters / chemistry
  • Filtration
  • Industrial Microbiology / methods
  • Ions
  • Kinetics
  • Lipase / chemistry*
  • Lipase / isolation & purification*
  • Metals / chemistry
  • Phylogeny
  • Solvents / chemistry

Substances

  • Butyrates
  • Esters
  • Ions
  • Metals
  • Solvents
  • Carbon
  • Lipase
  • ethyl butyrate