Title: Alternative Sweeteners

34 Auerbach et al.
Figure 2 Main degradation pathways of alitame.
to all peptides bearing N-terminal aspartic acid (4), also occurs to give the βaspartic
isomer of alitame. This rearranged dipeptide hydrolyzes at a slower rate
than alitame to give the same products as those arising from the parent compound
(i.e., aspartic acid and alanine amide). No cyclization to diketopiperazine or hydrolysis
of the alanine amide bond is detectable in solutions of alitame that have
undergone up to 90% decomposition. All three major decomposition products
are completely tasteless at levels that are possible in foods.
VI. STABILITY
In Fig. 3 the half-lives for alitame and aspartame (5) in buffer solutions of various
pH are compared. As can be seen, the solution stability of alitame approaches
the optimum for aspartic acid dipeptides. At acid pH (2–4), alitame solution halflives
are more than twice those of aspartame. As the pH increases, this stability
advantage increases dramatically. In particular in the neutral pH range (5–8)
alitame is completely stable for more than 1 year at room temperature.
Alitame is sufficiently stable for use in hard and soft candies, heat-pasteurized
foods, and in neutral pH foods processed at high temperatures, such as sweet
baked goods. The dramatic heat stability advantage of alitame over aspartame
under simulated baking conditions is illustrated in Fig. 4. Actual half-life data
for the two sweeteners under these conditions may be found in Table 3. This