Accéder au contenu
MilliporeSigma
Toutes les photos(2)

Documents

T7638

Sigma-Aldrich

Thaumatin from Thaumatococcus daniellii

Synonyme(s) :

Thaumatin Protein

Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme


About This Item

Code UNSPSC :
12352202
Nomenclature NACRES :
NA.56

Source biologique

plant (Thaumatococcus daniellii)

Forme

powder

Poids mol.

~22 kDa

Température de stockage

2-8°C

Description générale

Thaumatin is a super sweet protein extracted from the African plant katemfe, Thaumatococcus daniellii Benth. This non-toxic protein is a member of the broad family of pathogenesis-related proteins (group PR5). Thaumatin exists in five isoforms namely thaumatin I, II, III, a, and b.

Application

Thaumatin from Thaumatococcus daniellii has been used:
  • as a positive control/standard to detect the amount of recombinant thaumatin in the milk of transgenic mice using western blot
  • as a standard to compare its retention time with Vitis vinifera thaumatin-like proteins (VVTL1) occurring in free-run juice and determine the pathogenesis-related protein content in grape juices
  • as a model protein to study its interaction with free and ligated decavanadate

Actions biochimiques/physiologiques

Recently it was shown the over expression of the thaumatin gene from Thaumatococcus daniellii in tomatoes caused the fruit to have a sweeter taste, suggesting that thaumatin could be used to enhance the taste of various foods.
Thaumatin is a zero-calorie sweetener and flavor enhancer that finds its use in food industries. It has antifungal activity and elicits protective functions in plants. Thaumatin is useful in pharmaceutics as it is a constituent of special low-calorie diets.

Qualité

A mixture of thaumatin I and thaumatin II with traces of other sweet proteins.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Les clients ont également consulté

Modification of tomato taste in transgenic plants carrying a thaumatin gene from Thaumatococcus daniellii Benth.
Bartoszewski, G.
Plant Breeding, 122, 347-351 (2003)
Tetsuya Masuda et al.
Journal of bioscience and bioengineering, 102(5), 375-389 (2006-12-26)
Most proteins are tasteless and flavorless, while some proteins elicit a sweet-taste response on the human palate. Six proteins, thaumatin, monellin, mabinlin, brazzein, egg lysozyme, and neoculin (previously considered as curculin) have been identified as sweet-tasting proteins. However, no common
E C Zemanek et al.
Critical reviews in food science and nutrition, 35(5), 455-466 (1995-09-01)
The thaumatins are a class of intensely sweet proteins isolated from the fruit of the tropical plant Thaumatococcus danielli. Thaumatin is approved for use in many countries and has application as both a flavor enhancer and a high-intensity sweetener. The
P A Temussi
Cellular and molecular life sciences : CMLS, 63(16), 1876-1888 (2006-07-01)
A few proteins, discovered mainly in tropical fruits, have a distinct sweet taste. These proteins have played an important role towards a molecular understanding of the mechanisms of taste. Owing to the huge difference in size, between most sweeteners and
Chae Un Kim et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(12), 4596-4600 (2009-03-05)
Polymorphism of water has been extensively studied, but controversy still exists over the phase transition between high-density amorphous (HDA) and low-density amorphous (LDA) ice. We report the phase behavior of HDA ice inside high-pressure cryocooled protein crystals. Using X-ray diffraction

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

Contacter notre Service technique