http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&feed=atom&action=historyTeam:UC Davis/Project/Catalyst - Revision history2024-03-29T00:32:15ZRevision history for this page on the wikiMediaWiki 1.16.0http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=296934&oldid=prevNCsicsery at 03:07, 27 October 20122012-10-27T03:07:53Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We have designed and conducted three different experiments to determine (1) if the pelB tag is working to secrete the catalyst, (2) if the LC-cutinase protein is displaying its expected esterase behavior, and (3) if the protein is capable of breaking down PET from various sources.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We have designed and conducted three different experiments to determine (1) if the pelB tag is working to secrete the catalyst, (2) if the LC-cutinase protein is displaying its expected esterase behavior, and (3) if the protein is capable of breaking down PET from various sources.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><br>First, to determine where pelB-cutinase was being expressed, we cultured the pelB-cutinase-6His version of our construct. Beginning during exponential growth phase, we separated cells from the supernatant media at different time points, and ran samples on a western blot probing for the 6x-His tag. The details of this experiment can be found on the <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">protocols</a> page under "Cutinase Expression and Western Blot". <del class="diffchange diffchange-inline">Unfortunately, the blots contained significant amounts of background, which </del>is likely <del class="diffchange diffchange-inline">drowning out whatever signal exists</del>. <del class="diffchange diffchange-inline"> Thus we </del>currently <del class="diffchange diffchange-inline">do not have conclusive data as </del>to <del class="diffchange diffchange-inline">where pelB is transporting our catalyst</del>.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><br>First, to determine where pelB-cutinase was being expressed, we cultured the pelB-cutinase-6His version of our construct. Beginning during exponential growth phase, we separated cells from the supernatant media at different time points, and ran samples on a western blot probing for the 6x-His tag. The details of this experiment can be found on the <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">protocols</a> page under "Cutinase Expression and Western Blot". <ins class="diffchange diffchange-inline">The <a href="https://2012.igem.org/Team:UC_Davis/Data/Cutinase_Activity">results</a> show that pelB </ins>is likely <ins class="diffchange diffchange-inline">working as a secretion mechanism for cutinase</ins>. <ins class="diffchange diffchange-inline">We are </ins>currently <ins class="diffchange diffchange-inline">conducting more westerns </ins>to <ins class="diffchange diffchange-inline">better characterize the expression and secretion of the gene</ins>.<br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br>Second, we attempted to see if the Cutinase gene was exhibiting any esterase activity. This was done using a p-nitrophenol butyrate (pNPB) assay in hopes of evaluating and quantifying the esterase activity. pNPB is a monomer similar to the plastic PET that is cut by esterases in the same way. The benefit of the pNPB however is that as it is cut, the solution's absorbance at 405nm increases. This can be easily measured using a plate reader. The protocol for this assay was taken from literature and can be found on our <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">protocols page</a> under "pNPB Assay"[4]. </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br>Second, we attempted to see if the Cutinase gene was exhibiting any esterase activity. This was done using a p-nitrophenol butyrate (pNPB) assay in hopes of evaluating and quantifying the esterase activity. pNPB is a monomer similar to the plastic PET that is cut by esterases in the same way. The benefit of the pNPB however is that as it is cut, the solution's absorbance at 405nm increases. This can be easily measured using a plate reader. The protocol for this assay was taken from literature and can be found on our <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">protocols page</a> under "pNPB Assay"[4]. </div></td></tr>
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</table>NCsicseryhttp://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=266999&oldid=prevColson09 at 03:28, 4 October 20122012-10-04T03:28:20Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br>Second, we attempted to see if the Cutinase gene was exhibiting any esterase activity. This was done using a p-nitrophenol butyrate (pNPB) assay in hopes of evaluating and quantifying the esterase activity. pNPB is a monomer similar to the plastic PET that is cut by esterases in the same way. The benefit of the pNPB however is that as it is cut, the solution's absorbance at 405nm increases. This can be easily measured using a plate reader. The protocol for this assay was taken from literature and can be found on our <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">protocols page</a> under "pNPB Assay"[4]. </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br>Second, we attempted to see if the Cutinase gene was exhibiting any esterase activity. This was done using a p-nitrophenol butyrate (pNPB) assay in hopes of evaluating and quantifying the esterase activity. pNPB is a monomer similar to the plastic PET that is cut by esterases in the same way. The benefit of the pNPB however is that as it is cut, the solution's absorbance at 405nm increases. This can be easily measured using a plate reader. The protocol for this assay was taken from literature and can be found on our <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">protocols page</a> under "pNPB Assay"[4]. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Although this assay is usually done with purified esterases, we have had difficulties up to this point purifying cutinase. We did test, however, the activity of whole cells of our induced, uninduced, constitutive, and mutant constructs. Though these results gave us a general outline of the activity of each construct and of cutinase itself it’s important to note that these results only show general esterase activity and cannot necessarily be expected to parallel results with PET itself. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Although this assay is usually done with purified esterases, we have had difficulties up to this point purifying cutinase. We did test, however, the activity of whole cells of our induced, uninduced, constitutive, and mutant constructs <ins class="diffchange diffchange-inline">(our data is posted <a href="https://2012.igem.org/Team:UC_Davis/Data/Cutinase_Activity">here</a>)</ins>. Though these results gave us a general outline of the activity of each construct and of cutinase itself it’s important to note that these results only show general esterase activity and cannot necessarily be expected to parallel results with PET itself. </div></td></tr>
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</table>Colson09http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=264838&oldid=prevColson09 at 02:11, 4 October 20122012-10-04T02:11:21Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Experiments</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Experiments</p></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>We mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>We mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]<ins class="diffchange diffchange-inline">. We are currently working on comparing growth rates between these different enzyme forms by running cultures in a Tecan</ins>. <br><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>We <del class="diffchange diffchange-inline">are using </del>these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and <del class="diffchange diffchange-inline">modulating the </del>production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>We <ins class="diffchange diffchange-inline">expressed </ins>these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101 <ins class="diffchange diffchange-inline">(a constitutive promoter)</ins></a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000 <ins class="diffchange diffchange-inline">(pBad- an arabinose-inducible promoter)</ins></a> promoters to see the difference in overproduction of the enzymes<ins class="diffchange diffchange-inline">. We wanted to use an inducible promoter to finely control how much enzyme is expressed, </ins>and <ins class="diffchange diffchange-inline">our goal is to compare this controlled enzymatic </ins>production <ins class="diffchange diffchange-inline">against the constitutive promoter. We are also testing these construct in 96-well Tecan plates as well</ins>. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td></tr>
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</table>Colson09http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=264658&oldid=prevColson09 at 02:02, 4 October 20122012-10-04T02:02:22Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol, an excreted product. In addition, a mutant from the paper aforementioned was able to live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol, an excreted product. In addition, a mutant from the paper aforementioned was able to live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. </div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Unlike reductase, glycolaldehyde dehydrogenase is a protein that already favors aerobic conditions. <del class="diffchange diffchange-inline">THis </del>dehydrogenase oxidizes glycolaldehyde further to glycolate, and the glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Unlike reductase, glycolaldehyde dehydrogenase is a protein that already favors aerobic conditions. <ins class="diffchange diffchange-inline">This </ins>dehydrogenase oxidizes glycolaldehyde further to glycolate, and the glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <ins class="diffchange diffchange-inline"><br></ins><br></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Experiments</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Experiments</p></div></td></tr>
</table>Colson09http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=264639&oldid=prevColson09 at 02:01, 4 October 20122012-10-04T02:01:46Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol, an excreted product. In addition, a mutant from the paper aforementioned was able to live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol, an excreted product. In addition, a mutant from the paper aforementioned was able to live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. </div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><br><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del class="diffchange diffchange-inline">In contrast to the </del>reductase, glycolaldehyde dehydrogenase is <del class="diffchange diffchange-inline">an aerobic </del>protein that oxidizes glycolaldehyde further to glycolate<del class="diffchange diffchange-inline">. The </del>glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins class="diffchange diffchange-inline">Unlike </ins>reductase, glycolaldehyde dehydrogenase is <ins class="diffchange diffchange-inline">a </ins>protein that <ins class="diffchange diffchange-inline">already favors aerobic conditions. THis dehydrogenase </ins>oxidizes glycolaldehyde further to glycolate<ins class="diffchange diffchange-inline">, and the </ins>glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Experiments</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Experiments</p></div></td></tr>
</table>Colson09http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=264569&oldid=prevColson09 at 01:59, 4 October 20122012-10-04T01:59:01Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol, an excreted product. In addition, a mutant from the paper aforementioned was able to live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol, an excreted product. In addition, a mutant from the paper aforementioned was able to live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. </div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins style="color: red; font-weight: bold; text-decoration: none;"><br><br></ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins style="color: red; font-weight: bold; text-decoration: none;">In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br></ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Experiments</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><p>Experiments</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del style="color: red; font-weight: bold; text-decoration: none;">In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br><br></del></div></td><td colspan="2"> </td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
</table>Colson09http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=264480&oldid=prevColson09 at 01:55, 4 October 20122012-10-04T01:55:08Z<p></p>
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<td colspan='2' style="background-color: white; color:black;">Revision as of 01:55, 4 October 2012</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>coli</I> strains such as MG1655 can use it as an energy source (2). <br><br><a href="https://static.igem.org/mediawiki/2012/d/db/UCDavis_Construct1_large.jpg" class="lightbox"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>coli</I> strains such as MG1655 can use it as an energy source (2). <br><br><a href="https://static.igem.org/mediawiki/2012/d/db/UCDavis_Construct1_large.jpg" class="lightbox"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><img src="https://static.igem.org/mediawiki/2012/0/04/UCDavis_Construct1.png" width="600"></a><br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><img src="https://static.igem.org/mediawiki/2012/0/04/UCDavis_Construct1.png" width="600"></a><br><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol, an excreted product. In addition, a mutant from the paper aforementioned was able to live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. We <del class="diffchange diffchange-inline">are </del>mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol, an excreted product. In addition, a mutant from the paper aforementioned was able to live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. </div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> </div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins class="diffchange diffchange-inline"><p>Experiments</p></ins></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>We mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br><br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td></tr>
</table>Colson09http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=264388&oldid=prevColson09: Undo revision 264314 by Colson09 (talk)2012-10-04T01:50:35Z<p>Undo revision 264314 by <a href="/Special:Contributions/Colson09" title="Special:Contributions/Colson09">Colson09</a> (<a href="/wiki/index.php?title=User_talk:Colson09&action=edit&redlink=1" class="new" title="User talk:Colson09 (page does not exist)">talk</a>)</p>
<table style="background-color: white; color:black;">
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<td colspan='2' style="background-color: white; color:black;">← Older revision</td>
<td colspan='2' style="background-color: white; color:black;">Revision as of 01:50, 4 October 2012</td>
</tr><tr><td colspan="2" class="diff-lineno">Line 1,256:</td>
<td colspan="2" class="diff-lineno">Line 1,256:</td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>coli</I> strains such as MG1655 can use it as an energy source (2). <br><br><a href="https://static.igem.org/mediawiki/2012/d/db/UCDavis_Construct1_large.jpg" class="lightbox"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>coli</I> strains such as MG1655 can use it as an energy source (2). <br><br><a href="https://static.igem.org/mediawiki/2012/d/db/UCDavis_Construct1_large.jpg" class="lightbox"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><img src="https://static.igem.org/mediawiki/2012/0/04/UCDavis_Construct1.png" width="600"></a><br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><img src="https://static.igem.org/mediawiki/2012/0/04/UCDavis_Construct1.png" width="600"></a><br><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol <del class="diffchange diffchange-inline">and can </del>live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. We are mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol<ins class="diffchange diffchange-inline">, an excreted product. In addition, a mutant from the paper aforementioned was able to </ins>live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. We are mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br><br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td></tr>
</table>Colson09http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=264372&oldid=prevColson09: Undo revision 264363 by Colson09 (talk)2012-10-04T01:49:51Z<p>Undo revision 264363 by <a href="/Special:Contributions/Colson09" title="Special:Contributions/Colson09">Colson09</a> (<a href="/wiki/index.php?title=User_talk:Colson09&action=edit&redlink=1" class="new" title="User talk:Colson09 (page does not exist)">talk</a>)</p>
<table style="background-color: white; color:black;">
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<td colspan='2' style="background-color: white; color:black;">← Older revision</td>
<td colspan='2' style="background-color: white; color:black;">Revision as of 01:49, 4 October 2012</td>
</tr><tr><td colspan="2" class="diff-lineno">Line 1,256:</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>coli</I> strains such as MG1655 can use it as an energy source (2). <br><br><a href="https://static.igem.org/mediawiki/2012/d/db/UCDavis_Construct1_large.jpg" class="lightbox"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>coli</I> strains such as MG1655 can use it as an energy source (2). <br><br><a href="https://static.igem.org/mediawiki/2012/d/db/UCDavis_Construct1_large.jpg" class="lightbox"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><img src="https://static.igem.org/mediawiki/2012/0/04/UCDavis_Construct1.png" width="600"></a><br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><img src="https://static.igem.org/mediawiki/2012/0/04/UCDavis_Construct1.png" width="600"></a><br><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol<del class="diffchange diffchange-inline">, an excreted product. In addition, a mutant from the paper aforementioned was able to </del>live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. We are mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol <ins class="diffchange diffchange-inline">and can </ins>live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. We are mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br><br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td></tr>
</table>Colson09http://2012.igem.org/wiki/index.php?title=Team:UC_Davis/Project/Catalyst&diff=264363&oldid=prevColson09: Undo revision 264314 by Colson09 (talk)2012-10-04T01:49:28Z<p>Undo revision 264314 by <a href="/Special:Contributions/Colson09" title="Special:Contributions/Colson09">Colson09</a> (<a href="/wiki/index.php?title=User_talk:Colson09&action=edit&redlink=1" class="new" title="User talk:Colson09 (page does not exist)">talk</a>)</p>
<table style="background-color: white; color:black;">
<col class='diff-marker' />
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<col class='diff-marker' />
<col class='diff-content' />
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<td colspan='2' style="background-color: white; color:black;">← Older revision</td>
<td colspan='2' style="background-color: white; color:black;">Revision as of 01:49, 4 October 2012</td>
</tr><tr><td colspan="2" class="diff-lineno">Line 1,256:</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>coli</I> strains such as MG1655 can use it as an energy source (2). <br><br><a href="https://static.igem.org/mediawiki/2012/d/db/UCDavis_Construct1_large.jpg" class="lightbox"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>coli</I> strains such as MG1655 can use it as an energy source (2). <br><br><a href="https://static.igem.org/mediawiki/2012/d/db/UCDavis_Construct1_large.jpg" class="lightbox"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><img src="https://static.igem.org/mediawiki/2012/0/04/UCDavis_Construct1.png" width="600"></a><br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><img src="https://static.igem.org/mediawiki/2012/0/04/UCDavis_Construct1.png" width="600"></a><br><br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol <del class="diffchange diffchange-inline">and can </del>live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. We are mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><a name="Aerobic">Glycolaldehyde</a> reductase (DL-1,2-propanediol oxidoreductase) is normally an anaerobic protein that reduces L-lactaldehyde into L-1,2-propanediol<ins class="diffchange diffchange-inline">, an excreted product. In addition, a mutant from the paper aforementioned was able to </ins>live on L-1,2-propanediol as a sole carbon source. Not only are there mutants that live on the L-1,2-propanediol, but there are also mutants selected for growth on ethylene glycol. We are mutated one version of reductase to work optimally under aerobic conditions, rather than under anaerobic conditions. We got the idea to mutate the enzyme from the scientific literature, and we mutated reductase by using site directed mutagenesis (the protocol we used can be found <a href="https://2012.igem.org/Team:UC_Davis/Notebook/Protocols">here</a>) [3]. <br><br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In contrast to the reductase, glycolaldehyde dehydrogenase is an aerobic protein that oxidizes glycolaldehyde further to glycolate. The glycolate will be used further downstream in metabolism to provide the carbon source for the <I>E. coli</I> to live. <br><br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>We are using these enzymes polycistronically with the <a href="http://partsregistry.org/Part:BBa_J23101">Bba_J23101</a> and <a href="http://partsregistry.org/Part:BBa_K206000">Bba_K206000</a> promoters to see the difference in overproduction of the enzymes and modulating the production. Our modular efforts in plasmids will eventually be applied toward a rational strain engineering approach, where we manipulate the MG1655 chromosome to optimize the degradation of ethylene glycol. <br><br></div></td></tr>
</table>Colson09