In this study, the lipase gene of B. amyloliquefaciens E1PA
was successfully cloned and expressed in E. coli. The lipase gene
sequence of the E1PA strain is highly similar to that of B. amyloliquefaciens.
The moderately thermotolerant E1PA lipase exhibited
hydrolytic activity at extreme pH levels and a broad range of substrate
specificity. Effective reduction of oil and grease in lipid-rich
food debris wastewater by the E1PA strain indicated its ability to
grow and survive in this extreme environment. Once induced by
IPTG, the recombinant strain was able to produce lipase during its
growth, and the recombinant enzyme was relatively stable for up to
30 h.Additionally,the recombinantlipase exhibited functional lipid
hydrolysis activity that was higher than that of the wild-type E1PA
lipase. Taken together, these characteristics could render the E1PA
lipase as a good candidate as a biocatalyst for biodiesel production
utilizing inexpensive cooking oil or lipid-rich food waste. Such
substrates could also be used for lipase production by B. amyloliquefaciens
E1PA. Alternatively, E. coli expressing this lipase could be
further developed for the potential production of effective recombinant
E1PA lipase