Difference between revisions of "Part:BBa K4227002"
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<p>Natural monellin is a sweet protein obtained from the West African forest plant <i>Dioscoreophyllum cumminsii</i> Diels. It is 3,000 times sweeter than sucrose on a weight basis and can be used in industry as a sweetener and a flavor enhancer. It has some important advantages over artificial sweeteners. It is low in calories, safe, and neither introduces nonnatural metabolites into the body nor perturbs the balance of the amino acid pool as decomposition of the protein results in a natural distribution of all amino acids.<sup>[1]</sup> </p> | <p>Natural monellin is a sweet protein obtained from the West African forest plant <i>Dioscoreophyllum cumminsii</i> Diels. It is 3,000 times sweeter than sucrose on a weight basis and can be used in industry as a sweetener and a flavor enhancer. It has some important advantages over artificial sweeteners. It is low in calories, safe, and neither introduces nonnatural metabolites into the body nor perturbs the balance of the amino acid pool as decomposition of the protein results in a natural distribution of all amino acids.<sup>[1]</sup> </p> | ||
<p>The <i>Bacillus subtilis</i> was engineered by us to use as the oral probiotics. So, we design this part monellin to be a report module in the users' mouths. When the monellin was expressed, the user will taste the sweetness. </p> | <p>The <i>Bacillus subtilis</i> was engineered by us to use as the oral probiotics. So, we design this part monellin to be a report module in the users' mouths. When the monellin was expressed, the user will taste the sweetness. </p> | ||
| − | + | <h3><strong>Characterization</strong></h3> | |
<p><strong> (The following experimental data are from the literature and modeling, not the actual data made by the experiment) </strong></p> | <p><strong> (The following experimental data are from the literature and modeling, not the actual data made by the experiment) </strong></p> | ||
| − | + | ||
| − | <p>Since our experiment is severely influenced by COVID-19 in experimenter, materials, equipment and so on this year. We have to collect these data by the literature</p> | + | |
| + | <p>Since our experiment is severely influenced by COVID-19 in experimenter, materials, equipment and so on this year. We have to collect these data by the literature and modeling</p> | ||
<p><strong>We knew from the literature</strong> that natural monellin consists of two polypeptides containing 45 amino acid residues and 50 amino acid residues. Weak noncovalent bonds hold the two chains together. It is easily dissociated by heat or pH changes. </p> | <p><strong>We knew from the literature</strong> that natural monellin consists of two polypeptides containing 45 amino acid residues and 50 amino acid residues. Weak noncovalent bonds hold the two chains together. It is easily dissociated by heat or pH changes. </p> | ||
| − | <p>So | + | <p>So in order to use the monellin as a report molecule, we choose a kind of single strain monellin in which the two polypeptides are connected by a glycine residue, was designed and was found to be more stable under extreme heat and pH conditions without changing its sweetness. <sup>[2]</sup></p> |
<div style="display: flex;justify-content:center;align-items:center;flex-direction: column;"> | <div style="display: flex;justify-content:center;align-items:center;flex-direction: column;"> | ||
<div> | <div> | ||
<img src="https://static.igem.org/mediawiki/parts/2/29/Monellin_1.png"> | <img src="https://static.igem.org/mediawiki/parts/2/29/Monellin_1.png"> | ||
</div> | </div> | ||
| − | <p style="text-align: center;">Fig 1. The improvement of the stable under extreme heat and pH conditions [ | + | <p style="text-align: center;">Fig 1. The improvement of the stable under extreme heat and pH conditions.<sup>[2]</sup></p> |
</div> | </div> | ||
</html> | </html> | ||
===Modeling=== | ===Modeling=== | ||
| − | <p> | + | <html> |
| + | <p>Our modeling was based on the law of mass action.</p> | ||
| + | <div style="display: flex;justify-content:center;align-items:center;flex-direction: column;"> | ||
| + | <div> | ||
| + | <img width="900" height="auto" src="https://static.igem.org/mediawiki/parts/5/5f/Monellin_2.png"> | ||
| + | </div> | ||
| + | <p style="text-align: center;">Fig 2. The expression level of the monellin.</p> | ||
| + | </div> | ||
<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
| + | </html> | ||
<partinfo>BBa_K4227002 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4227002 SequenceAndFeatures</partinfo> | ||
===Reference=== | ===Reference=== | ||
| − | <p>[1]Zhongjun Chen, Cai Heng, Zhengying Li, Xinle Liang, Shangguan Xinchen. Expression and secretion of a single-chain sweet protein monellin in Bacillus subtilis by sacB promoter and signal peptide. | + | <p>[1] Zhongjun Chen, Cai Heng, Zhengying Li, Xinle Liang, Shangguan Xinchen. Expression and secretion of a single-chain sweet protein monellin in Bacillus subtilis by sacB promoter and signal peptide. Applied Microbiology and Biotechnology.2007;6 (73) : 1377-1381.</p> |
| − | <p>[2]Sung-Hou Kim, Chui-Hee Kang, Rosalind Kim, Joong Myung Cho, Yong-Beom Lee, Tae-Kyu Lee. Redesigning a sweet protein: increased stability and renaturability. | + | <p>[2] Sung-Hou Kim, Chui-Hee Kang, Rosalind Kim, Joong Myung Cho, Yong-Beom Lee, Tae-Kyu Lee. Redesigning a sweet protein: increased stability and renaturability. "Protein Engineering, Design and Selection".1989;8 (2) : 571-575.</p> |
<!-- Uncomment this to enable Functional Parameter display | <!-- Uncomment this to enable Functional Parameter display | ||
===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K4227002 parameters</partinfo> | <partinfo>BBa_K4227002 parameters</partinfo> | ||
<!-- --> | <!-- --> | ||
Latest revision as of 08:39, 8 October 2023
Monellin
ZJUT-China 2022's contribution
Usage and Biology
Natural monellin is a sweet protein obtained from the West African forest plant Dioscoreophyllum cumminsii Diels. It is 3,000 times sweeter than sucrose on a weight basis and can be used in industry as a sweetener and a flavor enhancer. It has some important advantages over artificial sweeteners. It is low in calories, safe, and neither introduces nonnatural metabolites into the body nor perturbs the balance of the amino acid pool as decomposition of the protein results in a natural distribution of all amino acids.[1]
The Bacillus subtilis was engineered by us to use as the oral probiotics. So, we design this part monellin to be a report module in the users' mouths. When the monellin was expressed, the user will taste the sweetness.
Characterization
(The following experimental data are from the literature and modeling, not the actual data made by the experiment)
Since our experiment is severely influenced by COVID-19 in experimenter, materials, equipment and so on this year. We have to collect these data by the literature and modeling
We knew from the literature that natural monellin consists of two polypeptides containing 45 amino acid residues and 50 amino acid residues. Weak noncovalent bonds hold the two chains together. It is easily dissociated by heat or pH changes.
So in order to use the monellin as a report molecule, we choose a kind of single strain monellin in which the two polypeptides are connected by a glycine residue, was designed and was found to be more stable under extreme heat and pH conditions without changing its sweetness. [2]
Fig 1. The improvement of the stable under extreme heat and pH conditions.[2]
Modeling
Our modeling was based on the law of mass action.
Fig 2. The expression level of the monellin.
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Reference
[1] Zhongjun Chen, Cai Heng, Zhengying Li, Xinle Liang, Shangguan Xinchen. Expression and secretion of a single-chain sweet protein monellin in Bacillus subtilis by sacB promoter and signal peptide. Applied Microbiology and Biotechnology.2007;6 (73) : 1377-1381.
[2] Sung-Hou Kim, Chui-Hee Kang, Rosalind Kim, Joong Myung Cho, Yong-Beom Lee, Tae-Kyu Lee. Redesigning a sweet protein: increased stability and renaturability. "Protein Engineering, Design and Selection".1989;8 (2) : 571-575.