Purification of lipase from Pseudomonas aeruginosa (from both a washed cell suspension and crude culture supernatant as the enzyme source) was performed utilizing affinity chromatography. Affinity chromatography was carried out using n-dodecylamine bound to Sepharose 4B. Chromatography of the concentrated crude culture supernatant resulted in a 65 to 95 fold purification with 5.8% recovery. Washed cells collected from a ten hour culture suspended in water also produced enzyme. Activity of the washed cell suspension supernatant was found to be 4.5 fold higher than the activity of the culture supernatant. A thirty percent recovery was obtained using the washed cell suspension supernatant. The washed cell suspension provides a cleaner preparation for use with the dodecylamine-agarose chromatography in purifying the enzyme.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc798171 |
| Date | 05 1900 |
| Creators | Morrison, Linda Kay |
| Publisher | North Texas State University |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | v, 57 leaves : ill., Text |
| Rights | Public, Morrison, Linda Kay, Copyright, Copyright is held by the author, unless otherwise noted. All rights |
Page generated in 0.0023 seconds