T7638
Thaumatin from Thaumatococcus daniellii
Synonym(s):
Thaumatin Protein
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All Photos(2)
About This Item
UNSPSC Code:
12352202
NACRES:
NA.56
Recommended Products
biological source
plant (Thaumatococcus daniellii)
form
powder
mol wt
~22 kDa
storage temp.
2-8°C
General description
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
Biochem/physiol Actions
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.
Quality
A mixture of thaumatin I and thaumatin II with traces of other sweet proteins.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Expression of functional plant sweet protein thaumatin II in the milk of transgenic mice
Lu R, et al.
Food and Bioproducts Processing, 125, 222-227 (2021)
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
Aleksey Firsov et al.
Protein expression and purification, 123, 1-5 (2016-03-12)
Thaumatin, a supersweet protein from the African plant katemfe (Thaumatococcus daniellii Benth.), is a promising zero-calorie sweetener for use in the food and pharmaceutical industries. Due to limited natural sources of thaumatin, its production using transgenic plants is an advantageous
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
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