Difference between revisions of "Team:Korea U Seoul/Design"

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<div class="container-fluid page-heading" style="background-image: url(https://static.igem.org/mediawiki/2016/5/53/Group.jpg)">
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    <h3>Design</h3>
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<h1>Design: Gelectricell</h1>
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<h3>★  ALERT! </h3>
 
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<p>This page is used by the judges to evaluate your team for the <a href="https://2016.igem.org/Judging/Awards#Special_Prizes"> design special prize</a>. </p>
 
  
  
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<p> Delete this box in order to be evaluated for this medal. See more information at <a href="https://2016.igem.org/Judging/Pages_for_Awards/Instructions"> Instructions for Pages for awards</a>.</p>
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<p>Our EMFC has 3 main systems.</p>  
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By talking about your design work on this page, there is one medal criterion that you can attempt to meet, and one award that you can apply for. If your team is going for a gold medal by building a functional prototype, you should tell us what you did on this page.
 
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<h2>1.Agar degradation</h2>
  
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<p>This is a prize for the team that has developed a synthetic biology product to solve a real world problem in the most elegant way. The students will have considered how well the product addresses the problem versus other potential solutions, how the product integrates or disrupts other products and processes, and how its lifecycle can more broadly impact our lives and environments in positive and negative ways.</p>
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<p>We used 3 enzymes to degrade agar in our device which are, Agarase, NABH (Neoagarobiose hydrolase), and AHGD (anhydrogalactose dehydrogenase).</p>
  
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<p>Agar is first degraded into neoagarobiose  by agarase. Neoagarosebiose is then degraded into D-galactose and 3.6-anhydro-L-galactose by NABH. 3.6-anhydro-L-galactose is then oxidized by NAD(P)+ dependent AHGD producing NAD(P)H.</p>
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If you are working on art and design as your main project, please join the art and design track. If you are integrating art and design into the core of your main project, please apply for the award by completing this page.
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<p>All listed enzymes are displayed on the surface of E.coli BW25113 using E.coli surface display vector pATLIC.</p>
  
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<p>Teams who want to focus on art and design should be in the art and design special track. If you want to have a sub-project in this area, you should compete for this award.</p>
 
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<h2>2. Shewanella oneidensis MR-1</h2>
  
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<p>Shewanella oneidensis MR-1 is a bacteria that can reduce metal instead of oxygen, thus generating electricity in a battery device.</p>
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<p>Shewanella oneidesis MR-1 is used in our device to generate electricity using D-galactose. However, Shewanella oneidensis MR-1 is known to be unable to use galactose as its carbon source. This is where co-cultured E.coli kicks in. E.coli BW25113 is able to utilize galactose to produce formate and acetate which Shewanella oneidensis MR-1 can utilize to generate electricity.</p>
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<h2>3. Diaphorase</h2>
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<p>Diaphorase is a type of enzyme that can generate electricity using NAD(P)H as the source of electron. It is expressed in BL21(DE3) with protein expression vector pB3.</p>
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<h2>References</h2>
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<li>Yun, Eun Ju, et al. "Production of 3, 6-anhydro-L-galactose from agarose by agarolytic enzymes of Saccharophagus degradans 2-40." Process biochemistry 46.1 (2011): 88-93.</li>
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<li>Yun, Eun Ju, et al. "The novel catabolic pathway of 3, 6‐anhydro‐L‐galactose, the main component of red macroalgae, in a marine bacterium." Environmental microbiology 17.5 (2015): 1677-1688.</li>
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<li>Ko, Hyeok-Jin, et al. "Functional cell surface display and controlled secretion of diverse agarolytic enzymes by Escherichia coli with a novel ligation-independent cloning vector based on the autotransporter YfaL." Applied and environmental microbiology 78.9 (2012): 3051-3058.</li>
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<li>Wang, Victor Bochuan, et al. "Metabolite-enabled mutualistic interaction between Shewanella oneidensis and Escherichia coli in a co-culture using an electrode as electron acceptor." Scientific reports 5 (2015).</li>
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Revision as of 01:28, 11 October 2016

Design

Design: Gelectricell

Our EMFC has 3 main systems.

1.Agar degradation

We used 3 enzymes to degrade agar in our device which are, Agarase, NABH (Neoagarobiose hydrolase), and AHGD (anhydrogalactose dehydrogenase).

Agar is first degraded into neoagarobiose by agarase. Neoagarosebiose is then degraded into D-galactose and 3.6-anhydro-L-galactose by NABH. 3.6-anhydro-L-galactose is then oxidized by NAD(P)+ dependent AHGD producing NAD(P)H.

All listed enzymes are displayed on the surface of E.coli BW25113 using E.coli surface display vector pATLIC.

2. Shewanella oneidensis MR-1

Shewanella oneidensis MR-1 is a bacteria that can reduce metal instead of oxygen, thus generating electricity in a battery device.

Shewanella oneidesis MR-1 is used in our device to generate electricity using D-galactose. However, Shewanella oneidensis MR-1 is known to be unable to use galactose as its carbon source. This is where co-cultured E.coli kicks in. E.coli BW25113 is able to utilize galactose to produce formate and acetate which Shewanella oneidensis MR-1 can utilize to generate electricity.

3. Diaphorase

Diaphorase is a type of enzyme that can generate electricity using NAD(P)H as the source of electron. It is expressed in BL21(DE3) with protein expression vector pB3.

References

  1. Yun, Eun Ju, et al. "Production of 3, 6-anhydro-L-galactose from agarose by agarolytic enzymes of Saccharophagus degradans 2-40." Process biochemistry 46.1 (2011): 88-93.
  2. Yun, Eun Ju, et al. "The novel catabolic pathway of 3, 6‐anhydro‐L‐galactose, the main component of red macroalgae, in a marine bacterium." Environmental microbiology 17.5 (2015): 1677-1688.
  3. Ko, Hyeok-Jin, et al. "Functional cell surface display and controlled secretion of diverse agarolytic enzymes by Escherichia coli with a novel ligation-independent cloning vector based on the autotransporter YfaL." Applied and environmental microbiology 78.9 (2012): 3051-3058.
  4. Wang, Victor Bochuan, et al. "Metabolite-enabled mutualistic interaction between Shewanella oneidensis and Escherichia coli in a co-culture using an electrode as electron acceptor." Scientific reports 5 (2015).