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Biodiesel can be produced by transesterification of oils using methanolysis in the presence of chemical or biological catalyst.
Lipase enzyme produced by Bacillus sp. isolated from a raw petrol sample was evaluated for its efficiency as a catalyst in the
production of biodiesel. The Bacillus spp. was identified by morphological, biochemical and physiological characteristics as Bacillus
stearothermophilus. The production of lipase enzyme by B. stearothermophilus was investigated and its properties were evaluated.
The enzyme exhibited moderate stability in organic solvents and seemed to be activated by isopropanol at a concentration of 25%
and 100%. The enzyme retained more than 94% of its activity in a buffer system supplied with ethylenediaminetetraacetic acid
(EDTA) compared to other metal ions investigated. The extracellular lipase enzyme from B. stearothermophilus was purified by
ammonium sulfate precipitation by bringing it to 40% saturation, followed by ion exchange chromatography. The SDS-PAGE of the
purified fraction showed two bands having a molecular mass of 35 and 50 kDa. The LC MS/MS analysis of the two bands revealed
no matches when searched against the NCBRI database suggesting that this lipase enzyme is a novel protein. The lipase enzyme
produced was used in the transesterification experiments to evaluate its efficiency as a biocatalyst for the production of biodiesel.
Four lipase preparations were used for the esterification of palm oil: Crude lipase, pure lipase, free enzyme from immobilized B.
stearothermophilus cells, and pure lipase immobilized in sodium alginate beads. Compared to chemical transesterification, the free
and pure form of lipase showed moderate efficiency to convert palm oil into biodiesel. The maximum yield of biodiesel obtained
was 70% when lipase from immobilized cells was employed which is considered valuable as it affects the cost of the production
process throughout the direct production of biodiesel.