Loading...
EXTRACELLULAR LIPASE OF PSEUDOMONAS AERUGINOSA
Jaeger, Karl-Erich Wohlfarth, Susanne Winkler, Ulrich K.
Jaeger, Karl-Erich
Wohlfarth, Susanne
Winkler, Ulrich K.
Citations
Altmetric:
Advisors
Editors
Other Contributors
Issue Date
1991
Submitted date
2024-03-27
Files
Loading...
PDF
Adobe PDF, 2.2 MB
Other Titles
Abstract
Lipase of Pseudomonas aeruginosa was excreted in form of high M,- aggregates consisting of protein and lipopolysaccharide. Solubilization and isoelectric focusing in the presence of the zwitterionic detergent CHAPS yielded in an electrophoretically pure lipase protein of M, 29 kDa with an isoelectric point of 5.9. Charge shift electrophoresis showed that lipase was an amphiphilic protein, its activity was dependent on the presence of detergent. Lipase cleaved a variety of different substrates showing no positional specificity. The lipase gene was cloned and sequenced revealing the lipase consensus sequence Gly-His-Ser-His-Gly. Polyclonal antibodies were raised against purified lipase having a titer of 1400 and a detection limit in the picogram range.
Citation
Lipases : structure, mechanism and genetic engineering, 381 - 384
DOI
PubMed ID
PubMed Central ID
Additional Links
Embedded video
Type
Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
EISSN
ISBN
156081165X
3527283323
3527283323
ISMN
Gov't Doc #
Sponsors
License
Attribution-NonCommercial-ShareAlike 4.0 International