|
|
| Line 7: |
Line 7: |
| | <h1 align=middle> Results </h1> | | <h1 align=middle> Results </h1> |
| | <div class="container"> | | <div class="container"> |
| − | <div class="row section">
| |
| − | <div class="col-xs-12 col-sm-8 col-md-8">
| |
| − | <!--<https://2017.igem.org/File:EsteraseResults3.png">-->
| |
| − | <img src="https://static.igem.org/mediawiki/2017/3/3a/EsteraseResults3.png" class="img-responsive"/>
| |
| − | <h8>Figure 5:Illustration of the esterase activity [U] of LipB in the supernatant dependend on time and substrate concentration (2.5, 5, 10, 15, 20 mM). The standard abbreviation was calculated from biological triplicates.
| |
| − | </h8>
| |
| − | </div>
| |
| − | <div class="col-xs-12 col-sm-4 col-md-4">
| |
| − | <p>Additionally we investigated the enzyme activity of LipB. To compare the enzyme activities of LipB and EstCS2, we used the same induction levels and substrate concentrations for the assays. The figures show that the enzyme activity of the supernatant isn’t higher than the enzyme activity of the supernatant of the wild type cells. These results can be declared with the absence of a signal peptide at the N-terminal side of the esterase gene. Thus, no enzyme secretion is performed and less enzyme activity can be detected in the supernatant. This leads to the conclusion that a signal peptide has to be added at the N-terminal side of the esterase gene to obtain enzyme secretion and extracellular enzyme activity.
| |
| − | </p>
| |
| − | </div>
| |
| − | </div>
| |
| | <div class="row section"> | | <div class="row section"> |
| | <h3>Keratinases</h3> | | <h3>Keratinases</h3> |
