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

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

Author information

1
BRD School of Biosciences, Sardar Patel Maidan, Sardar Patel University, Vallabh Vidyanagar, Gujarat, India. vdandavate@gmail.com

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.

PMID:
19285387
DOI:
10.1016/j.biortech.2009.02.011
[Indexed for MEDLINE]

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