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Accumulation of a recombinant Aspergillus oryzae lipase artificially localized on the Bacillus subtilis cell surface
cutL cDNA encoding an extracellular lipase, L1, from Aspergillus oryzae was fused to the cell wall-binding domain (CWB) region of a plasmid, pHCB3R. SDS-polyacrylamide gel electrophoresis (PAGE) and zymography of proteins extracted from the cell surface of Bacillus subtilis 168 harboring a fused lip...
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Published in: | Journal of bioscience and bioengineering 2000, Vol.90 (4), p.422-425 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | cutL cDNA encoding an extracellular lipase, L1, from
Aspergillus oryzae was fused to the cell wall-binding domain (CWB) region of a plasmid, pHCB3R. SDS-polyacrylamide gel electrophoresis (PAGE) and zymography of proteins extracted from the cell surface of
Bacillus subtilis 168 harboring a fused lipase plasmid (pHCB3RCL) revealed that the fused gene product, CWB-CutL, was localized in the
B. subtilis cell wall and retained lipase activity.
B. subtilis WASD (
wprA sigD), recently used for the accumulation of CWB-LipB (the CWB protein fused with
B. subtilis lipase B), was also a suitable host for the accumulation of CWB-CutL, the amount being 10% of the total proteins extracted from the cell surface. |
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ISSN: | 1389-1723 1347-4421 |
DOI: | 10.1016/S1389-1723(01)80012-8 |