Soma Japanese spaniel

Thaumatin I
Identifier
Cable address	THM1_THADA
PDB	1RQWRCSB PDB PDBe PDBj) More structures
UniProt	P02883

Thaumatin II
Identifier
Cable address	THM2_THADA
UniProt	P02884

Schematic view of soma Japanese spaniel I

The soma Japanese spaniel (with Thaumatin, the tau poison nut) is a low-calorie sweetener. This protein is used as a beauty conditioner other than a sweetener [¹].

The soma Japanese spaniel was discovered as a mixture of the protein isolated from fruit of plant, tau mark coxswain tick Eri (Thaumatococcus daniellii) of the maranta department of West Africa first. Approximately 2,000 times is more generous in the protein of the soma Japanese spaniel system sweetener than sugar. In addition, the taste of the soma Japanese spaniel of sweets is considerably very different from the sugar. The sweetness of the soma Japanese spaniel appears very slowly and leaves a licorice of aftertaste when I took it in in large quantities, and the sense continues for a long time. The soma Japanese spaniel is easy to dissolve in water very much and is stable in heat and acid environment.

Table of contents

Biological role

The production of soma Japanese spaniels is derived in response to the attack to the plant due to the viroid pathogen. Some of soma Japanese spaniel system protein inhibit growth and the sporulation of the spawn of various bacteria in vitro. The soma Japanese spaniel is regarded as the prototype of the disease-causing germs reply protein domain. This soma Japanese spaniel domain is distributed over the wide creature to rice and カエノラブディティス elegance. It is protein in conjunction with the attack mechanism (PR), and soma Japanese spaniels are derived by a thing ranging from ethylene to a pathogen, and I am maldistributed [²], and so poison nut, osmotin, cigarette measure and minor PR protein, α-amylase / trypsin in crack terequal が are included in the whole plant by overuse structurally. These protein participates in the systematic resistant acquisition and stress reply of the plant, but do not understand the accurate role [²]. The soma Japanese spaniel is approximately 100,000 times [³] of sucrose and very sweet protein on the basis of mols. Soma Japanese spaniel I is comprised of 207 residues with single stranded polypeptide.

Like other PR protein, it is predicted that the soma Japanese spaniel has β structure that a lot of β turns have few ヘリックス [²]. The cell of the cigarette which I exposed to the environment where I gradually nominated salt concentration for enlarges salt tolerance by expression of オスミチン drastically [⁴]. The wheat which infected an udon powder disease-causing bacteria develops PRIR2 and comes to have tolerance for the infection [⁵]. It is suggested that the PR protein acts as a certain repressor from soybean α - amylase / trypsin in crack terとの similarity of this PR protein and other PR protein [⁵].

What decrease by heating is shown without the protein of soma Japanese spaniel isolated from kiwi fruit and an apple decreasing the property as the allergen by the digestion with the stomach and intestines too much [⁶]; [⁷].

Production, use

In West Africa, tau mark coxswain tick Eri is cultivated locally and is used for the seasoning of food and the drink. The seed of the fruit is surrounded by seed-coverings, and this becomes the source of the soma Japanese spaniel. In the 1970s, Tate & Lyle started the extraction of the soma Japanese spaniel from fruit. In 1990, the researcher of Unilever performed an isolation, sequencing of two basic protein in a soma Japanese spaniel and was reported when I named soma Japanese spaniel I, soma Japanese spaniel II. This researcher was able to produce a soma Japanese spaniel with the genetically-modified bacteria.

The soma Japanese spaniel is authorized as a sweetener in European Union (E957), Israel, Japan. In the United States of America, I am recognized as a safe flavoring agent (FEMA GRAS 3732), but am not recognized for a sweetener. Because the soma Japanese spaniel has not only the sweetness but also masking action to reduce unpleasant taste such as the bitterness, the enhancing action to raise flavor, I am used for not only the food but also pharmaceutical products [⁸].

Crystal

The soma Japanese spaniel crystallizes in the presence of a tartaric acid ion rapidly and easily, and soma Japanese spaniel - tartaric acid mixture is used as a model system of the protein crystallization frequently. Interestingly, the solubility of the soma Japanese spaniel, a crystal habit, the crystal formation mechanism depend on the chirality of the precipitant to use. When I crystallize with L-tartaric acid, the soma Japanese spaniel forms both drills type crystal, and the solubility increases with temperature. In the case of D-and meso- tartaric acid, I form a prism-formed crystal, and the solubility decreases with temperature [⁹]. This suggests that control of the chirality of the precipitant generally becomes the important factor in protein crystallization.

Allied item

• クルクリン
• Mirach phosphorus
• Monellin
• Stevia

Source

1. ^ Green C (1999). "Thaumatin: a natural flavour ingredient." World Rev Nutr Diet. It is 129–32. doi: World Review of Nutrition and Dietetics 85 10.1159/000059716. ISBN 3-8055-6938-6. PMID 10647344. 
2. ^ ^{a b c} Herrera-Estrella L, Ruiz-Medrano R, Jimenez-Moraila B, Rivera-Bustamante RF (1992). "Nucleotide sequence of an osmotin-like cDNA induced in tomato during viroid infection." Plant Mol. Biol. 20 (6): 1199–1202. doi: 10.1007/BF00028909. PMID 1463856. 
3. ^ Edens L, Heslinga L, Klok R, Ledeboer MNJ, Toonen MY, Visser C, Verrips CT (1982). "Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli." Gene 18 (1): 1–12. doi: 10.1016/0378-1119(82) 90,050-6. PMID 7049841. 
4. ^ Singh NK, Nelson DE, Kuhn D, Hasegawa PM, Bressan RA (1989). "Molecular Cloning of Osmotin and Regulation of Its Expression by ABA and Adaptation to Low Water Potential". Plant Physiol. 90 (3): 1096–1101. doi: 10.1104/pp.90.3.1096. PMC 1061849. It is http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1061849. PMID 16666857 
5. ^ ^{a b} Rebmann G, Mauch F, Dudler R, Hertig C, Bull J (1991). "A wheat glutathione-S-transferase gene with transposon-like sequences in the promoter region." Plant Mol. Biol. 16 (6): 1089–1091. doi: 10.1007/BF00016083. PMID 1650615. 
6. ^ Bublin M, Radauer C, Knulst A, Wagner S, Scheiner O, Mackie AR, Mills EN, Breiteneder H., Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein. Mol Nutr Food Res. 2008 Oct; 52(10): 1130-9.
7. ^ Smole U, Bublin M, Radauer C, Ebner C, Breiteneder H., Mal d 2, the thaumatin-like allergen from apple, is highly resistant to gastrointestinal digestion and thermal processing. Int Arch Allergy Immunol. 2008, 147 (4): 289-98. Epub 2008 Jul 11.
8. ^ スイートナー laboratory、Three Sakae source F F eyes
9. ^ Asherie, Ginsberg, Greenbaum, Blass and Knafo. Effects of Protein Purity and Precipitant Stereochemistry on the Crystallization of Thaumatin, Crystal Growth and Design, Volume 8, issue 12 (December 3, 2008), p. 4200-4207. ISSN 1528-7483 DOI: 10.1021/cg800616q

Allied documents

• Higginbotham JD (1986). Gelardi RC, Nabors LO. ed. Alternative sweeteners. New York: M. Dekker, Inc. ISBN 0-8247-7491-4. 
• Higginbotham J, Witty M (1994). Thaumatin. Boca Raton: CRC Press. ISBN 0-8493-5196-0. 

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