Title: Alternative Sweeteners

36 Auerbach et al.
allows alitame to survive the thermal and pH conditions of the baking process
with insignificant decomposition.
VII. COMPATIBILITY
Alitame exhibits excellent functionality and is compatible with a wide variety of
freshly prepared foods. In accordance with its chemical structure, it can undergo
chemical reaction with certain food components. In particular, high levels of reducing
sugars, such as glucose and lactose, may react with alitame in heated
liquid or semiliquid systems, such as baked goods, to form Maillard reaction
products. High levels of flavor aldehydes can behave similarly. Such reactions
have been reported for aspartame and other aspartyl dipeptides (6–9). Therefore,
the compatibility of alitame with a given recipe will depend on the actual ingredients
present and the thermal and pH exposure involved in the manufacturing
process.
Prolonged storage of alitame in a few standard acidic liquid beverages recipes
may result in an incompatibility as measured organoleptically (off-flavors).
This is not reflected in storage stability as measured by chemical assay for alitame
and its degradation products. Levels of off-flavorant(s) are below the limits of
modern analytical detection. Substances, which may produce off-flavors on storage
with alitame in liquid products, are hydrogen peroxide, sodium bisulfite,
ascorbic acid, and some types of caramel color at pHs less than 4.0. However,
a research program is underway to find appropriate solutions to overcome these
problems.
VIII. METABOLISM
After oral administration to the mouse, rat, dog, or man, alitame is well absorbed.
Most of an oral dose (77–96%) is excreted in urine as a mixture of metabolites
(Fig. 5). The remainder (7–22%) is excreted in the feces, primarily as unchanged
alitame. Radiochemical balances of 97–105% were obtained in the four species.
In all four species the metabolism of alitame is characterized by the loss
of aspartic acid followed by conjugation and/or oxidation at the sulfur atom of
the alanine amide fragment yielding the corresponding sulfoxide isomers and the
sulfone. Further hydrolysis of the alanine amide fragments does not take place.
In the rat and dog the alanine amide is partially acetylated, and in man it is
partially conjugated with glucuronic acid. No observable cleavage of the alanine
amide bond or rupture of the thietane ring takes place.
Because the aspartic acid portion of the molecule is available for normal
amino acid metabolism, alitame is partially caloric. The maximum caloric contri-