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− | <h1>Favorite Basic Part</h1> | + | <h1>Favorite Basic Part: BBa_k2139003</h1> |
<img src="https://static.igem.org/mediawiki/2016/9/95/T--British_Columbia--Outline.png" | <img src="https://static.igem.org/mediawiki/2016/9/95/T--British_Columbia--Outline.png" | ||
− | align="left"; width="500px"; style="padding-right:10px; margin-bottom: 25px; max-width: 100%"><p align="justify"> | + | 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_K2139003"> BBa_K2139003</a> is comprised of the coding region of E1. E1 was used as a fusion protein within the middle of <i>Caulobacter cresentus’s</i> RSA-A surface layer protein. We were able to show expression on the surface of <i>C. crescentus</i> and functionally characterize that it maintained functionality. You can see our data here. The part originated from <i>AcidoThermus cellulolyticus</i> and was codon optimized for expression in <i> C. crescentus</i>. Our biobrick contains only the catalytic domain of the full protein.</p> |
− | <p align="justify"> | + | <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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Revision as of 02:15, 18 October 2016
Basic Part
Favorite Basic Part: BBa_k2139003
BBa_K2139003 is comprised of the coding region of E1. E1 was used as a fusion protein within the middle of Caulobacter cresentus’s RSA-A surface layer protein. We were able to show expression on the surface of C. crescentus and functionally characterize that it maintained functionality. You can see our data here. The part originated from AcidoThermus cellulolyticus and was codon optimized for expression in C. crescentus. Our biobrick contains only the catalytic domain of the full protein.
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.
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.
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.
Check out other parts of our project below!