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

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</style><!--navigation menu -->
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<table class="gwd-table-nb4m editable" width="100%">
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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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      <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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      <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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      <a href="https://2015.igem.org/Team:San_Andres/Notebook"
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style="color: rgb(0, 0, 0);"> Statistics</a>
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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>
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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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      <a href="https://2015.igem.org/Team:San_Andres/Modeling"
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style="color: rgb(0, 0, 0);"> Metodology</a>
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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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      <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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      <a href="https://igem.org/Team_List?year=2015"><img
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<h1>Enzymes</h1>
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<big>During our investigation we sought the perfect enzyme to
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degrade the gluten, and we found:<br>
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</big>
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<ul>
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  <li><big>Prolyl Endopeptidase: It is a kind of serine
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protease capable of breaking peptide bonds following to the group of
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terminal carboxyl of a PROLINE residue. While he was a candidate for a
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possible treatment failed to meet expectations, because its activity is
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a high pH, which is not suitable for an average digestive. Another
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reason was that it degrades slowly, which would have resulted in a
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longer and inefficient treatment.</big></li>
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</ul>
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<div style="text-align: center;"><img
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alt="File:Prolil.jpg"
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src="https://static.igem.org/mediawiki/2015/c/c0/Prolil.jpg"
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height="376" width="565"><br>
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<br>
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<div style="text-align: left;">
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<ul>
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  <li><big>Kumamolisin As: It is the first known example of
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a collagenase derived from the family of the sedolisin. This operates
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at high temperatures and low pH levels. Its characteristics, together
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with those predicted are measured by comparison between a collagenase
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and a peptidase from serine, which are related to the enzyme
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preference, to thus Digest collagen as gluten.</big></li>
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</ul>
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<div style="text-align: center;"><img
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alt="File:2-2-2 2.jpg"
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src="https://static.igem.org/mediawiki/2015/b/be/2-2-2_2.jpg"
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height="243" width="470"><br>
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<ul style="text-align: left;">
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  <li><big>KumaMax (G319S, D358G, D368H, N281D): It is a
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mutation of the Kumamolisin As, which is designed to digest way more
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efficient gluten, because that can work at pH levels much more lower
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than the original enzyme (a pH of 4.0) which is excellent for the
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average digestive system. <span class="hps">It was
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created by the team IGEM Washington 2011</span>. Other advantages
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are:</big></li>
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</ul>
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<ol style="text-align: left;">
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  <li><big>It is resistant to high temperatures and acidity
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of the stomach.</big></li>
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  <li><big>It is heat stable, in others words, it is
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resistant to all changes in their physical and chemical structure.</big></li>
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  <li><big>It is easily repairable and creable.</big></li>
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</ol>
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<div style="text-align: center;"><img
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alt="File:175px-Washington Bottle.jpg"
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src="https://static.igem.org/mediawiki/2015/d/d0/175px-Washington_Bottle.jpg"
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height="263" width="175"> <img
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alt="File:250px-Washington Kumamolisin VS SC-PEP.png"
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src="https://static.igem.org/mediawiki/2015/1/1b/250px-Washington_Kumamolisin_VS_SC-PEP.png"
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height="213" width="250">&nbsp;<img
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alt="File:250px-Washington Kuma Bonded triad.png"
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src="https://static.igem.org/mediawiki/2015/6/62/250px-Washington_Kuma_Bonded_triad.png"
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height="193" width="250"></div>
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<br>
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<div style="text-align: left;"><big><br>
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</big>
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<div style="text-align: center;">
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<div style="text-align: center;"><span id="result_box"
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class="" lang="en"><span class="hps"></span><span
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Latest revision as of 02:02, 23 July 2015