| Literature DB >> 25163839 |
Jae-Hyung Jo1, Chan-Wook Han, Seung-Hwan Kim, Hyuk-Jin Kwon, Hyune-Hwan Lee.
Abstract
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.Entities:
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Year: 2014 PMID： 25163839 DOI： 10.1007/s12275-014-4217-7
Source DB: PubMed Journal: J Microbiol ISSN： 1225-8873 Impact factor: 3.422