miraculin

The idea of the "miraculin party" was conceived then.

Miraculin works by binding to the sweet receptors on the tongue.

This can continue for about an hour while the miraculin protein is still bound to the taste receptor.

This effect is due to miraculin, which is used commercially as a sugar substitute.

Miraculin's effect lasts as long as the protein is bound to the tongue, which can be up to an hour.

On the other hand, two plant proteins, miraculin and curculin, cause sour foods to taste sweet.

Within each dimer 2 miraculin glycoproteins are linked by a disulfide bridge.

It contains a glycoprotein molecule, with some trailing carbohydrate chains, called miraculin.

While curculin has some innate sweet taste of its own, miraculin is by itself quite tasteless.

Glycoprotein is sensitive to heat: when heated over 100 C, miraculin loses its taste-modifying property.

It has been suggested that the miraculin protein can change the structure of taste receptors on the cells of the tongue.

Two grams of lettuce leaves produced roughly the same amount of miraculin as in one miracle fruit berry.

Because miraculin is denatured by heating, the pulp must be preserved without heating for commercial use.

The scientists' crops resulted in 40 micrograms of miraculin per gram of lettuce leaves, which was considered a large amount.

The anti-sweet compound, Gymnemic acid suppresses the sweet taste of miraculin, like it does for sucrose.

Once the acidic food is swallowed, miraculin returns to its inactive shape until the next acidic food comes along.

However, after the taste buds are exposed to miraculin, ordinarily sour foods, such as citrus, are perceived as sweet.

Miraculin activity is inactivated at pH below 3 and pH above 12 at room temperature.

Purification and some properties of miraculin, a glycoprotein from Synsepalum dulcificum which provokes sweetness and blocks sourness.

The taste modifying protein, miraculin, has seven cystein residues in a molecule composed of 191 amino acid residues.

As already known miraculin binds strongly to the sweet taste receptors on our tongues; however, it does not activate receptors at neutral pH.

As miraculin is a readily soluble protein and relatively heat stable, it is a potential sweetener in acidic food (e.g. soft drinks).

However, on the eve of the product's launch in 1974 the FDA determined that miraculin would be considered a food additive and thus require years more testing.

Like miraculin, curculin exhibits taste-modifying activity; however, unlike miraculin, it also exhibits a sweet taste by itself.

"Human Sweet Taste Receptor Mediates Acid-Induced Sweetness of Miraculin."