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Team:TP CC-SanDiego/Project.html
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<div id="third-text"> <p align="justify"> <br><br><br> Our idea is to attach signal peptides to the N-terminus of the detoxifying enzymes. We use <a href="http://www.signalpeptide.com/index.php?sess=&m=listspdb_bacteria&s=details&id=37&listname="> alpha amylase signal peptides</a> and | <div id="third-text"> <p align="justify"> <br><br><br> Our idea is to attach signal peptides to the N-terminus of the detoxifying enzymes. We use <a href="http://www.signalpeptide.com/index.php?sess=&m=listspdb_bacteria&s=details&id=37&listname="> alpha amylase signal peptides</a> and | ||
<a href="http://www.signalpeptide.com/index.php?sess=&m=listspdb_bacteria&s=details&id=34&listname="> beta-lactamase signal peptides</a>. The original proteins for these signal peptides are <br><br><br><br> secreted out naturally by E. Coli, especially in strain K that we use for our project. They both follow sec-dependent pathways. In the case of beta-lactamase signal protein, cases have been shown of successful fusion proteins <br><br><br><br> <a href="http://www.ncbi.nlm.nih.gov/pubmed/6607473">secreted</a> by the beta-lactamase signal protein. Successful continual excretion of the mycotoxin degradation enzymes can be purified in mass amounts periodically, or the chimeric E. Coli can be placed directly on<br> <br><br><br>crops to prevent and combat mycotoxin exposure. Since there is no cure to mycotoxin exposure, enhanced prevention with successful secretion will be very influential. </p></div> | <a href="http://www.signalpeptide.com/index.php?sess=&m=listspdb_bacteria&s=details&id=34&listname="> beta-lactamase signal peptides</a>. The original proteins for these signal peptides are <br><br><br><br> secreted out naturally by E. Coli, especially in strain K that we use for our project. They both follow sec-dependent pathways. In the case of beta-lactamase signal protein, cases have been shown of successful fusion proteins <br><br><br><br> <a href="http://www.ncbi.nlm.nih.gov/pubmed/6607473">secreted</a> by the beta-lactamase signal protein. Successful continual excretion of the mycotoxin degradation enzymes can be purified in mass amounts periodically, or the chimeric E. Coli can be placed directly on<br> <br><br><br>crops to prevent and combat mycotoxin exposure. Since there is no cure to mycotoxin exposure, enhanced prevention with successful secretion will be very influential. </p></div> | ||
Revision as of 19:35, 20 June 2014
Background
The Project Background and Explanation
The Project Background and Explanation
AflatoxinB1-Detoxifizyme is produced by Armillariella Tabescens intracellularly. Its gene is analyzed to have no introns and has been recombined into a plasmid before. Extraction is rather difficult and commercialization has not been able to be done yet.
Zearalenone Hydorlase is produced by Clonostachys Rosea. Its gene is also analyzed to have no introns and has been recombined into a plasmid before. Similar to ADTZ, commercialization has not been done yet.
Natural E. coli secretes various proteins by signal peptides that recognize translocons. We focus on the SEC pathway that lets the protein fold in the periplasm first, as it usually results in more correct folding, correct formation of disulfide bridges, minimizes degradation, and is less likely to result in accumulation.
Idea
E. Coli Capable of Extracelluar Secretion of Mycotoxin Detoxifying Enzymes
E. Coli Capable of Extracelluar Secretion of Mycotoxin Detoxifying Enzymes
Our idea is to attach signal peptides to the N-terminus of the detoxifying enzymes. We use alpha amylase signal peptides and
beta-lactamase signal peptides. The original proteins for these signal peptides are
secreted out naturally by E. Coli, especially in strain K that we use for our project. They both follow sec-dependent pathways. In the case of beta-lactamase signal protein, cases have been shown of successful fusion proteins
secreted by the beta-lactamase signal protein. Successful continual excretion of the mycotoxin degradation enzymes can be purified in mass amounts periodically, or the chimeric E. Coli can be placed directly on
crops to prevent and combat mycotoxin exposure. Since there is no cure to mycotoxin exposure, enhanced prevention with successful secretion will be very influential.
How
The Process to Complete our Project
;"
The Process to Complete our Project
Our idea is to attach signal peptides to the N-terminus of the detoxifying enzymes. We use alpha amylase signal peptides and
beta-lactamase signal peptides. The original proteins for these signal peptides are
secreted out naturally by E. Coli, especially in strain K that we use for our project. They both follow sec-dependent pathways. In the case of beta-lactamase signal protein, cases have been shown of successful fusion proteins
secreted by the beta-lactamase signal protein. Successful continual excretion of the mycotoxin degradation enzymes can be purified in mass amounts periodically, or the chimeric E. Coli can be placed directly on
crops to prevent and combat mycotoxin exposure. Since there is no cure to mycotoxin exposure, enhanced prevention with successful secretion will be very influential.
Attributions
Teamwork, education, and assistance
Teamwork, education, and assistance
The TP_CC-SanDiego iGEM Team came up with the idea during its brainstorming meetings and performed the laboratory work. The team made group decisions about the direction of the project, troubleshooted, and put together the data and presentation.
The Simpson Joseph Laboratory of UCSD provided us the space, equipments and various reagents that allowed the students to perform the web laboratory work. The people of the Joseph Lab gave the team many tips and protocols. The Jeff Hasty Laboratory of UCSD provided the team and others lectures and past iGEM experiences that helped them greatly.
Dr. Chang-Ho Baek from Thermo Fisher mentored us throughout the project, gave us lectures, gave us advice for troubleshooting when there were obstacles. Thermo Fisher provided us various reagent donations.
