T7638
Thaumatin from Thaumatococcus daniellii
Synonym(s):
Thaumatin Protein
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About This Item
NACRES:
NA.56
UNSPSC Code:
12352202
Form:
powder
Biological source:
plant (Thaumatococcus daniellii)
Mol wt:
~22 kDa
biological source
plant (Thaumatococcus daniellii)
form
powder
mol wt
~22 kDa
storage temp.
2-8°C
Quality Level
Analysis Note
A mixture of thaumatin I and thaumatin II with traces of other sweet proteins.
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.
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
动植物源性产品
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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
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)
Tuning the interactions of decavanadate with thaumatin, lysozyme, proteinase K and human serum proteins by its coordination to a pentaaquacobalt (ii) complex cation
Krivosudsky L, et al.
New. J. Chem., 43(45), 17863-17871 (2019)
Isabelle Martiel et al.
Acta crystallographica. Section D, Structural biology, 77(Pt 9), 1153-1167 (2021-09-03)
Serial data collection has emerged as a major tool for data collection at state-of-the-art light sources, such as microfocus beamlines at synchrotrons and X-ray free-electron lasers. Challenging targets, characterized by small crystal sizes, weak diffraction and stringent dose limits, benefit
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