Difference between revisions of "Team:British Columbia/Achievements/Parts/Composite Part"

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<h1>Favorite Composite Part: BBa_k2139005</h1>
 
<h1>Favorite Composite Part: BBa_k2139005</h1>
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align="left"; width="500px"; style="padding-right:10px; margin-bottom: 25px; max-width: 100%"><p align="justify"> <a href= "http://parts.igem.org/wiki/index.php?title=Part:BBa_K2139005"> BBa_K2139005</a> is the expression cassette of the basic part <a href= "http://parts.igem.org/wiki/index.php?title=Part:BBa_K2139003"> BBa_K2139003</a> that was used to do the surface expression experiments in <i>C. crescentus</i>. Although we were un-able to functionally characterize it during our project due to time constraints (characterized as fusion protein see data here), it has been well documented in literature which can be found below.</p>
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<p align="justify"><a href= "http://parts.igem.org/wiki/index.php?title=Part:BBa_K2139005"> BBa_K2139005</a> is the expression cassette of the basic part <a href= "http://parts.igem.org/wiki/index.php?title=Part:BBa_K2139003"> BBa_K2139003</a> that was used to do the surface expression experiments in <i>C. crescentus</i>. Although we were un-able to functionally characterize it during our project due to time constraints (characterized as fusion protein see data here), it has been well documented in literature which can be found below.</p>
  
 
<p align="justify">The construct was designed to contain the Ptac promotor, ribosome binding site, coding region, and double terminator. This was to allow for the constitutive expression of the enzyme. The catalytic function of the enzyme is to convert XXXXXX to YYYYYY.
 
<p align="justify">The construct was designed to contain the Ptac promotor, ribosome binding site, coding region, and double terminator. This was to allow for the constitutive expression of the enzyme. The catalytic function of the enzyme is to convert XXXXXX to YYYYYY.
  
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<p align="justify">References: Linger, Jeffrey G., William S. Adney, and Al Darzins. "Heterologous Expression and Extracellular Secretion of Cellulolytic Enzymes by Zymomonas Mobilis." Applied and Environmental Microbiology, vol. 76, no. 19, 2010., pp. 6360-6369doi:10.1128/AEM.00230-10.
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<p align="justify"><b>References:</b> Linger, Jeffrey G., William S. Adney, and Al Darzins. "Heterologous Expression and Extracellular Secretion of Cellulolytic Enzymes by Zymomonas Mobilis." Applied and Environmental Microbiology, vol. 76, no. 19, 2010., pp. 6360-6369doi:10.1128/AEM.00230-10.
 
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<p align="justify">    One successfully implemented solution has been to use microbial biocatalysts to transform renewable biomass, from agricultural and forestry wastes, into bio-equivalent chemicals able to be directly used in established industrial processes. Companies such as BioAmber and Genomatica have championed this approach, creating important molecular building blocks such as succinic acid and 1,4-butanediol. While these early successes have highlighted the potential of these systems, renewable biomass as a whole remains underutilized. However, major roadblock to implementing successful industrial-scale bio-processes is the high cost of processing raw biomass into a usable form. Comprising greater than 50 percent of total production costs, as estimated by the National Renewable Energy Lab, biomass processing creates a significant barrier that prevents all but the most mature technologies from utilizing renewable feedstocks.
 
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<p align="justify">    This year, our team aimed to bring the processing of biomass back to BC mills by making the utilization of renewable biomass feed stocks cheaper and more efficient. Taking lessons from nature, we pursued a bio-mimicry approach, aiming to build a microbial community able to effectively transform biomass into useful products. To accomplish this task, we split our microbial community into two halves. One half responsible for transforming the biomass into usable growth substrates. While the other half focuses on using these growth substrates for the production of useful products. Our community has the potential to provide an unique method for surface display of functional enzymes, while also being a proof of concept for the direct conversion of raw biomass into usable products.</p>
 
  
 
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Revision as of 07:49, 18 October 2016

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Overview

Composite Part

Favorite Composite Part: BBa_k2139005

BBa_K2139005 is the expression cassette of the basic part BBa_K2139003 that was used to do the surface expression experiments in C. crescentus. Although we were un-able to functionally characterize it during our project due to time constraints (characterized as fusion protein see data here), it has been well documented in literature which can be found below.

The construct was designed to contain the Ptac promotor, ribosome binding site, coding region, and double terminator. This was to allow for the constitutive expression of the enzyme. The catalytic function of the enzyme is to convert XXXXXX to YYYYYY.

References: Linger, Jeffrey G., William S. Adney, and Al Darzins. "Heterologous Expression and Extracellular Secretion of Cellulolytic Enzymes by Zymomonas Mobilis." Applied and Environmental Microbiology, vol. 76, no. 19, 2010., pp. 6360-6369doi:10.1128/AEM.00230-10.

Check out other parts of our project below!