Purification and Characterization of Lipase from Rhizomucor miehei

Gangaraju Uvarani, Lakshmanan Jaganathan, Preetha Shridas, Rathanam Boopathy

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


The production of Rhizomucor miehei lipase by solid state fermentation by growing the fungi for 5 days at room temperature on wheat bran medium with a moisture content of 0.75 mL/g is described. The purification of this extracellular enzyme to apparent homogeneity employing a two-step purification sequence using ion-exchange and Octyl-Sepharose affinity chromatography with 135-fold purity and 12% recovery is reported. The purified extracellular enzyme displays maximum activity at pH 7.0 and 65°C. The characteristic feature of this enzyme is its thermostability, retaining 90% of its activity upon exposure to 65°C for 30 min. Further, organic solvents like ethanol and acetone have a stimulatory effect on the lipase activity. But, metal ions such as Mg2+, Mn2+, Co2+, Zn2+, Hg2+ and Fe2+ or EDTA, p-chloromercuric benzoate each at 1mM concentration have a profound inhibitory effect on its catalytic activity. These properties together with its stability in organic solvents could form a basis for further characterization of the enzyme as a potential candidate for exploitation at industrial level.

Original languageEnglish
Pages (from-to)607-610
Number of pages4
JournalJournal of Scientific and Industrial Research
Issue number10-11
StatePublished - 1998

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Purification and Characterization of Lipase from Rhizomucor miehei'. Together they form a unique fingerprint.

Cite this