Difference between revisions of "Team:San Andres/Experiments"

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{{San_Andres}}
 
 
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<h2>Experiments &amp; Protocols</h2>
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<p>Describe the experiments, research and protocols you used in your iGEM project.</p>
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<h5>What should this page contain?</h5>
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<img src="https://static.igem.org/mediawiki/2015/0/09/Firma_800.jpg"
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</style><!--navigation menu -->
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<table class="gwd-table-nb4m editable" width="100%">
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  <tbody>
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    </tr>
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onmouseover="this.bgColor='#ffba00'"
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onmouseout="this.bgColor='#fcff00'" align="center"
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bgcolor="#fcff00" height="45">
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      <a href="https://2015.igem.org/Team:San_Andres"
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style="color: rgb(0, 0, 0);">Home </a> </td>
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      <td style="border: 2px solid black;"
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onmouseout="this.bgColor='#fcff00'" align="center"
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      <a href="https://2015.igem.org/Team:San_Andres/Team"
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style="color: rgb(0, 0, 0);"> Team </a> </td>
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      <td style="border: 2px solid black;"
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      <a href="https://2015.igem.org/Team:San_Andres/Description"
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style="color: rgb(0, 0, 0);"> Project </a>
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      </td>
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      <td style="border: 2px solid black;"
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onmouseover="this.bgColor='#ffba00'"
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onmouseout="this.bgColor='#fcff00'" align="center"
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bgcolor="#fcff00" height="45">
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      <a href="https://2015.igem.org/Team:San_Andres/Notebook"
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style="color: rgb(0, 0, 0);"> Statistics</a>
 +
      </td>
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      <td style="border: 2px solid black;"
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onmouseover="this.bgColor='#ffba00'"
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onmouseout="this.bgColor='#fcff00'" align="center"
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      <a href="https://2015.igem.org/Team:San_Andres/Experiments"
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style="color: rgb(0, 0, 0);"> Enzymes</a>
 +
      </td>
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      <td style="border: 2px solid black;"
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      <a href="https://2015.igem.org/Team:San_Andres/Parts"
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style="color: rgb(0, 0, 0);"> Parts</a>
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      </td>
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      <td style="border: 2px solid black;"
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onmouseover="this.bgColor='#ffba00'"
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onmouseout="this.bgColor='#fcff00'" align="center"
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      <a href="https://2015.igem.org/Team:San_Andres/Notebook"
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style="color: rgb(0, 0, 0);"> Metodology</a>
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      </td>
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      <a href="https://2015.igem.org/Team:San_Andres/Results"
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style="color: rgb(0, 0, 0);"> Results </a>
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      </td>
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      <td style="border: 2px solid black;"
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      <a href="https://2015.igem.org/Team:San_Andres/Collaborations"
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style="color: rgb(0, 0, 0);"> Future Projections </a>
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      </td>
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      <td align="center">
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      <a href="https://igem.org/Team_List?year=2015"><img
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src="https://static.igem.org/mediawiki/igem.org/6/60/Igemlogo_300px.png"
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width="55"></a></td>
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    </tr>
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  </tbody>
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<div class="gwd-div-2ed9"></div>
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<div class="gwd-div-7xzo gwd-a-1thu">
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<h1>Enzymes</h1>
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<big>During our investigation we sought the perfect enzyme to
 +
degrade the gluten, and we found:<br>
 +
</big>
 
<ul>
 
<ul>
−
<li> Protocols </li>
+
  <li><big>Prolyl Endopeptidase: It is a kind of serine
−
<li> Experiments </li>
+
protease capable of breaking peptide bonds following to the group of
−
<li>Documentation of the development of your project </li>
+
terminal carboxyl of a PROLINE residue. While he was a candidate for a
 +
possible treatment failed to meet expectations, because its activity is
 +
a high pH, which is not suitable for an average digestive. Another
 +
reason was that it degrades slowly, which would have resulted in a
 +
longer and inefficient treatment.</big></li>
 
</ul>
 
</ul>
−
 
+
<div style="text-align: center;"><img
−
 
+
alt="File:Prolil.jpg"
−
 
+
src="https://static.igem.org/mediawiki/2015/c/c0/Prolil.jpg"
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<h4>Inspiration</h4>
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height="376" width="565"><br>
 +
<br>
 +
<div style="text-align: left;">
 
<ul>
 
<ul>
−
<li><a href="https://2014.igem.org/Team:Colombia/Protocols">2014 Colombia </a></li>
+
  <li><big>Kumamolisin As: It is the first known example of
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<li><a href="https://2014.igem.org/Team:Imperial/Protocols">2014 Imperial </a></li>
+
a collagenase derived from the family of the sedolisin. This operates
−
<li><a href="https://2014.igem.org/Team:Caltech/Project/Experiments">2014 Caltech </a></li>
+
at high temperatures and low pH levels. Its characteristics, together
 +
with those predicted are measured by comparison between a collagenase
 +
and a peptidase from serine, which are related to the enzyme
 +
preference, to thus Digest collagen as gluten.</big></li>
 
</ul>
 
</ul>
 +
<div style="text-align: center;"><img
 +
alt="File:2-2-2 2.jpg"
 +
src="https://static.igem.org/mediawiki/2015/b/be/2-2-2_2.jpg"
 +
height="243" width="470"><br>
 +
<ul style="text-align: left;">
 +
  <li><big>KumaMax (G319S, D358G, D368H, N281D): It is a
 +
mutation of the Kumamolisin As, which is designed to digest way more
 +
efficient gluten, because that can work at pH levels much more lower
 +
than the original enzyme (a pH of 4.0) which is excellent for the
 +
average digestive system. <span class="hps">It was
 +
created by the team IGEM Washington 2011</span>. Other advantages
 +
are:</big></li>
 +
</ul>
 +
<ol style="text-align: left;">
 +
  <li><big>It is resistant to high temperatures and acidity
 +
of the stomach.</big></li>
 +
  <li><big>It is heat stable, in others words, it is
 +
resistant to all changes in their physical and chemical structure.</big></li>
 +
  <li><big>It is easily repairable and creable.</big></li>
 +
</ol>
 +
<div style="text-align: left;"><img
 +
alt="File:175px-Washington Bottle.jpg"
 +
src="https://static.igem.org/mediawiki/2015/d/d0/175px-Washington_Bottle.jpg"
 +
height="263" width="175"> <img
 +
alt="File:250px-Washington Kumamolisin VS SC-PEP.png"
 +
src="https://static.igem.org/mediawiki/2015/1/1b/250px-Washington_Kumamolisin_VS_SC-PEP.png"
 +
height="213" width="250">&nbsp;<img
 +
alt="File:250px-Washington Kuma Bonded triad.png"
 +
src="https://static.igem.org/mediawiki/2015/6/62/250px-Washington_Kuma_Bonded_triad.png"
 +
height="193" width="250"></div>
 +
<br>
 +
<div style="text-align: left;"></div>
 +
</div>
 +
</div>
 +
</div>
 +
<div style="text-align: left;"><br>
 +
<div style="text-align: center;"><br>
 +
<div style="text-align: left;"><big><br>
 +
</big>
 +
<div style="text-align: center;">
 +
<div style="text-align: center;"><span id="result_box"
 +
class="" lang="en"><span class="hps"></span><span
 +
class="hps"></span></span><br>
 +
</div>
 +
<span id="result_box" class="" lang="en"><span
 +
class="hps"></span></span></div>
 +
<span id="result_box" class="" lang="en"><span
 +
class="hps"><br>
 +
</span></span></div>
 +
</div>
 +
</div>
 +
</div>
 +
<div style="text-align: center;"><br>
 
</div>
 
</div>
 +
<div class="gwd-div-a9c8"></div>
 +
<br>
 +
</body>
 
</html>
 
</html>

Revision as of 20:01, 5 July 2015

wiki 2

Home Team Project Statistics Enzymes Parts Metodology Results Future Projections

Enzymes

During our investigation we sought the perfect enzyme to degrade the gluten, and we found:
  • Prolyl Endopeptidase: It is a kind of serine protease capable of breaking peptide bonds following to the group of terminal carboxyl of a PROLINE residue. While he was a candidate for a possible treatment failed to meet expectations, because its activity is a high pH, which is not suitable for an average digestive. Another reason was that it degrades slowly, which would have resulted in a longer and inefficient treatment.
File:Prolil.jpg

  • Kumamolisin As: It is the first known example of a collagenase derived from the family of the sedolisin. This operates at high temperatures and low pH levels. Its characteristics, together with those predicted are measured by comparison between a collagenase and a peptidase from serine, which are related to the enzyme preference, to thus Digest collagen as gluten.
File:2-2-2 2.jpg
  • KumaMax (G319S, D358G, D368H, N281D): It is a mutation of the Kumamolisin As, which is designed to digest way more efficient gluten, because that can work at pH levels much more lower than the original enzyme (a pH of 4.0) which is excellent for the average digestive system. It was created by the team IGEM Washington 2011. Other advantages are:
  1. It is resistant to high temperatures and acidity of the stomach.
  2. It is heat stable, in others words, it is resistant to all changes in their physical and chemical structure.
  3. It is easily repairable and creable.
File:175px-Washington Bottle.jpg File:250px-Washington Kumamolisin VS SC-PEP.png File:250px-Washington Kuma Bonded triad.png