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KMID : 0880220140520100856
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Journal of Microbiology
2014 Volume.52 No. 10 p.856 ~ p.862
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Surface display expression of Bacillus licheniformis lipase in Escherichia coli using Lpp’OmpA chimera
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Jo Jae-Hyung
Han Chan-Wook
Kim Seung-Hwan
Kwon Hyuk-Jin
Lee Hyune-Hwan
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Abstract
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The lipase from Bacillus licheniformis ATCC14580 was displayed on the cell surface of Escherichia coli using Lpp’OmpA as the anchoring protein. The expressed Lpp’OmpA-lipase fusion protein has a molecular weight of approximately 35 kDa, which was confirmed by SDS-PAGE and western blot analysis. The Lpp’OmpA-lipase fusion protein was located on the cell surface, as determined by immunofluorescence confocal microscopy and flow cytometry. The enzyme activity of the surface-displayed lipase showed clear halo around the colony. The cell surface-displayed lipase showed the highest activity of 248.12 ± 9.42 U/g (lyophilized cell) at the optimal temperature of 37°C and pH 8.0. The enzyme exhibited the highest activity toward the substrate p-nitrophenyl caprylate (C8). These results suggest that E. coli, which displayed the lipase on its surface, could be used as a whole cell biocatalyst.
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KEYWORD
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surface display, Bacillus lichenformis, lipase, Lpp’OmpA, Escherichia coli
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