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Team:Greensboro-Austin
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Taking advantage of muscle adhesive proteins (MAPs) really '''stuck on''' to this year’s UT iGEM team. Muscle adhesive proteins have amassed much attention as a potential adhesive for biomedical, underwater and other commercially relevant applications. Furthermore, muscle adhesive proteins are sought for their biodegradability, biocompatibility and ability to adhere to various substrates. However, production of muscle adhesive proteins proves to be an arduous task. Extraction-based production and in-vitro-based production are expensive, inefficient, and unsustainable. Thus, our team focused on improving the efficiency of in vivo production of MAPs utilizing fusion protein fp-151. MAPs derive their adhesive properties from the hydroxylation of tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA) then to dopaquinone. This project reprogrammed the stop codon to incorporate an unnatural amino acid L-DOPA. In turn, this technique provides tighter control of L-DOPA incorporation whereas previous in vivo projects, depending on posttranslational modification, contained a lesser yield of L-DOPA. Our team aims to develop the technology for large-scale MAP production in E. coli that will ultimately allow for rapid, cost-effective, and commercially viable production of an adhesive for biomedical applications. | Taking advantage of muscle adhesive proteins (MAPs) really '''stuck on''' to this year’s UT iGEM team. Muscle adhesive proteins have amassed much attention as a potential adhesive for biomedical, underwater and other commercially relevant applications. Furthermore, muscle adhesive proteins are sought for their biodegradability, biocompatibility and ability to adhere to various substrates. However, production of muscle adhesive proteins proves to be an arduous task. Extraction-based production and in-vitro-based production are expensive, inefficient, and unsustainable. Thus, our team focused on improving the efficiency of in vivo production of MAPs utilizing fusion protein fp-151. MAPs derive their adhesive properties from the hydroxylation of tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA) then to dopaquinone. This project reprogrammed the stop codon to incorporate an unnatural amino acid L-DOPA. In turn, this technique provides tighter control of L-DOPA incorporation whereas previous in vivo projects, depending on posttranslational modification, contained a lesser yield of L-DOPA. Our team aims to develop the technology for large-scale MAP production in E. coli that will ultimately allow for rapid, cost-effective, and commercially viable production of an adhesive for biomedical applications. | ||
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| - | + | As long animals have been domesticated, farmers have sought a solution to decreasing odor emissions with a close eye on cost-effectiveness. In swine manure, the worst culprit is the compound ''p''-cresol. To remedy this, UT iGEM is using engineered E. coli to degrade <i>p</i>-cresol down to Acetyl-CoA and pyruvate, two potential carbon sources for our bacteria to use for growth. Using directed evolution, strains with a high efficiency of degradation and the ability to use ''p''-cresol as their sole carbon source could be isolated. Ultimately, this strain could be potentially be used in probiotics for livestock and pets for odor reduction. | |
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Revision as of 07:22, 19 July 2013
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Project GluE coli
Taking advantage of muscle adhesive proteins (MAPs) really stuck on to this year’s UT iGEM team. Muscle adhesive proteins have amassed much attention as a potential adhesive for biomedical, underwater and other commercially relevant applications. Furthermore, muscle adhesive proteins are sought for their biodegradability, biocompatibility and ability to adhere to various substrates. However, production of muscle adhesive proteins proves to be an arduous task. Extraction-based production and in-vitro-based production are expensive, inefficient, and unsustainable. Thus, our team focused on improving the efficiency of in vivo production of MAPs utilizing fusion protein fp-151. MAPs derive their adhesive properties from the hydroxylation of tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA) then to dopaquinone. This project reprogrammed the stop codon to incorporate an unnatural amino acid L-DOPA. In turn, this technique provides tighter control of L-DOPA incorporation whereas previous in vivo projects, depending on posttranslational modification, contained a lesser yield of L-DOPA. Our team aims to develop the technology for large-scale MAP production in E. coli that will ultimately allow for rapid, cost-effective, and commercially viable production of an adhesive for biomedical applications.
Project "D. odori"
As long animals have been domesticated, farmers have sought a solution to decreasing odor emissions with a close eye on cost-effectiveness. In swine manure, the worst culprit is the compound p-cresol. To remedy this, UT iGEM is using engineered E. coli to degrade p-cresol down to Acetyl-CoA and pyruvate, two potential carbon sources for our bacteria to use for growth. Using directed evolution, strains with a high efficiency of degradation and the ability to use p-cresol as their sole carbon source could be isolated. Ultimately, this strain could be potentially be used in probiotics for livestock and pets for odor reduction.
