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| | <h2> The first step</h2> | | <h2> The first step</h2> |
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| − | Right now the team is working on a proof of concept. Our first Flexosome will contain <b>phosphatase, estherase</b>and <b>lipase</b> found in metagenomic libraries along with a fluorescent reporter gene. Once our E. coli is able to express and produce this functional Flexosome, this will open the door for more complex and specific applications. | + | Right now the team is working on a proof of concept. Our first Flexosome will contain <b>phosphatase, estherase</b> and <b>lipase</b> found in metagenomic libraries along with a fluorescent reporter gene. Once our E. coli is able to express and produce this functional Flexosome, this will open the door for more complex and specific applications. |
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| | <h2> The inspiration </h2> | | <h2> The inspiration </h2> |
Revision as of 17:50, 14 July 2015
About our Project
Our project
The
iGEM team Goettingen 2015 is currently developing “
Flexosome”
It is our
enzymatic penknife: a customizable complex for more efficient and
synergistic multi-enzymatic processes. It consists of a
scaffoldin, dockerins and
exchangeable enzymes.
The enzymes of interest can be attached to the scaffoldin via the dockerin stations and once attached complete the reactions.
The first step
Right now the team is working on a proof of concept. Our first Flexosome will contain
phosphatase, estherase and
lipase found in metagenomic libraries along with a fluorescent reporter gene. Once our E. coli is able to express and produce this functional Flexosome, this will open the door for more complex and specific applications.
The inspiration
We studied the natural
cellulosome structure, in which different cellulotytic enzymes are assembled into a bigger scaffoldin via dockerin stations, leading to optimized cellulose degradation. The interaction between scaffoldin and dockerins has been proven to be
strong and stable, this gave us the ideal platform to design our
"Flexosome” device.
Traditionally cellulosome engineering is thought for optimization of cellulose degradation, but we don’t have to stop there! A much broader range of enzymes are actively being discovered every year. That is why we intend to combine the scaffoldin protein from cellulolytic bacterium with varying and exchangeable enzymes. The result: a very
versatile, stable and innovative tool!
The goal
We want to achieve a protein construct which will be able to ensure a
high local concentration of enzymes and
catalyse multiple enzymatic processes at one site, making the product of one process the substrate of the next on the scaffoldin. Ultimately, the construct will not only
increase efficiency of the reactions but also be
fully customisable for any kind of enzymatic process.
References