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Neohesperidin dihydrochalcone[1]
Names
IUPAC name
1-[4-[[(2S,3R,4S,5S,6R)-4,5-Dihydroxy-6-(hydroxymethyl)-3-
[[(2S,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyl-2-
tetrahydropyranyl]oxy]-2-tetrahydropyranyl]oxy]-2,6-
dihydroxyphenyl]-3-(3-hydroxy-4-methoxyphenyl)propan-1-one
Identifiers
ChEBI CHEBI:83535
ChemSpider 28072
PubChem 30231
InChI[show]
SMILES[show]
Properties
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Infobox references
Thaumatin
From Wikipedia, the free encyclopedia
Thaumatin family
Ribbon[1][2] diagram of thaumatin I. From PDB:1RQW.
Identifiers
Symbol Thaumatin
Pfam PF00314
InterPro IPR001938
SMART SM00205
PROSITE PDOC00286
SCOP 1thu
SUPERFAMILY 1thu
CDD cd09215
Identifiers
Symbol THM1_THADA
UniProt P02883
Thaumatin II
Identifiers
Symbol THM2_THADA
UniProt P02884
Thaumatin is a low-calorie sweetener and flavour modifier. The protein is often used primarily for its
flavour-modifying properties and not exclusively as a sweetener.[3]
The thaumatins were first found as a mixture of proteins isolated from
the katemfe fruit (Thaumatococcus daniellii Bennett) of westAfrica. Some proteins in the thaumatin
family of sweeteners are roughly 2000 times more potent than sugar. Although very sweet,
thaumatin's taste is markedly different from sugar's. The sweetness of thaumatin builds very slowly.
Perception lasts a long time, leaving a liquorice-like aftertaste at high usage levels. Thaumatin is
highly water-soluble, stable to heating, and stable under acidic conditions.
Biological role[edit]
Thaumatin production is induced in katemfe in response to an attack upon the plant
by viroid pathogens. Several members of the thaumatin protein family display significant in
vitro inhibition of hyphal growth and sporulation by various fungi. The thaumatin protein is
considered a prototype for a pathogen-response protein domain. This thaumatin domain has been
found in species as diverse as rice and Caenorhabditis elegans. Thaumatins are pathogenesis-
related (PR) proteins, which are induced by various agents ranging from ethylene to pathogens, and
are structurally diverse and ubiquitous in plants:[4] They include thaumatin, osmotin, tobacco major
and minor PR proteins, alpha-amylase/trypsin inhibitor, and P21 and PWIR2 soybean and wheat leaf
proteins. The proteins are involved in systematically acquired resistance and stress response in
plants, although their precise role is unknown.[4] Thaumatin is an intensely sweet-tasting protein (on a
molar basis about 100,000 times as sweet as sucrose[5]) found in the West African
shrub Thaumatococcus daniellii: it is induced by attack by viroids, which are single-stranded
unencapsulated RNA molecules that do not code for protein. The thaumatin protein I consists of a
single polypeptide chain of 207 residues.
Like other PR proteins, thaumatin is predicted to have a mainly beta structure, with a high content of
beta-turns and little helix.[4]Tobacco cells exposed to gradually increased salt concentrations develop
a greatly increased tolerance to salt, due to the expression of osmotin,[6] a member of the PR protein
family. Wheat plants attacked by barley powdery mildew express a PR protein (PWIR2), which
results in resistance against that infection.[7] The similarity between this PR protein and other PR
proteins to the maize alpha-amylase/trypsin inhibitor has suggested PR proteins may act as some
form of inhibitor.[7]
The thaumatin-like proteins isolated from kiwi fruit or apple appear to have their allergenic properties
minimally reduced by gastroduodenal digestive processes, but not by heating.[8][9]
Production[edit]
Thaumatin crystal (~1mm long) grown by liquidliquid diffusion under microgravity conditions in outer space.
Arrow marks nucleation point.[10]
Within West Africa, the katemfe fruit has been locally cultivated and used to flavor foods and
beverages for some time. The fruit's seeds are encased in a membranous sac, or aril, that is the
source of thaumatin. In the 1970s, Tate and Lyle began extracting thaumatin from the fruit. In 1990,
researchers at Unilever reported the isolation and sequencing of the two principal proteins found in
thaumatin, which they dubbedthaumatin I and thaumatin II. These researchers were also able to
express thaumatin in genetically engineered bacteria.
Thaumatin has been approved as a sweetener in the European Union (E957), Israel, and Japan. In
the United States, it is generally recognized as safe as a flavoring agent (FEMA GRAS 3732) but not
as a sweetener.
Crystallization of thaumatin[edit]
Since thaumatin crystallizes rapidly and easily in the presence of tartrate ions, thaumatin-tartrate
mixtures are frequently used as model systems to study protein crystallization. Interestingly, the
solubility of thaumatin, its crystal habit, and mechanism of crystal formation are dependent upon
the chirality of precipitant used. When crystallized with L- tartrate, thaumatin forms bipyramidal
crystals and displays a solubility that increases with temperature; with D- and meso-tartrate, it forms
stubby and prismatic crystals and displays a solubility that decreases with temperature.[11]This
suggests control of precipitant chirality may be an important factor in protein crystallization in
general.