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      <a href="https://2015.igem.org/Team:San_Andres"
 style="color: rgb(0, 0, 0);">Home </a> </td>
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      <a href="https://2015.igem.org/Team:San_Andres/Team"
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      <a href="https://2015.igem.org/Team:San_Andres/Description"
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      <a href="https://2015.igem.org/Team:San_Andres/Notebook"
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      <a href="https://2015.igem.org/Team:San_Andres/Experiments"
 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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      <a href="https://2015.igem.org/Team:San_Andres/Notebook"
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      <a href="https://2015.igem.org/Team:San_Andres/Results"
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      <a href="https://2015.igem.org/Team:San_Andres/Collaborations"
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<h1>Enzymes</h1>
<big>During our investigation we sought the perfect enzyme to
degrade the gluten, and we found:<br>
</big>
<ul>
  <li><big>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.</big></li>
</ul>
<div style="text-align: center;"><img
 alt="File:Prolil.jpg"
 src="https://static.igem.org/mediawiki/2015/c/c0/Prolil.jpg"
 height="376" width="565"><br>
<br>
<div style="text-align: left;">
<ul>
  <li><big>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.</big></li>
</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"
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 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>
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