Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
