Literature DB >> 6591191

Racemization of aspartic acid and phenylalanine in the sweetener aspartame at 100 degrees C.

M F Boehm, J L Bada.   

Abstract

The racemization half-lives (i.e., the time required to reach a D/L = 0.33) at pH 6.8 for aspartic acid and phenylalanine in the sweetener aspartame (L-aspartyl-L-phenylalanine methyl ester) were determined to be 13 and 23 hours, respectively, at 100 degrees C. Racemization at this pH does not occur in aspartame but rather in its diketopiperazine decomposition product. Our results indicate that the use of aspartame to sweeten neutral pH foods and beverages that are then heated at elevated temperature could generate D-aspartic acid and D-phenylalanine. The nutritive consequences of these D-amino acids in the human diet are not well established, and thus aspartame should probably not be used as a sweetener when the exposure of neutral pH foods and beverages to elevated temperatures is required. At pH 4, a typical pH of most foods and beverages that might be sweetened with aspartame, the half-lives are 47 hours for aspartic acid and 1200 hours for phenylalanine at 100 degrees C. Racemization at pH 4 takes place in aspartame itself. Although the racemization rates at pH 4 are slow and no appreciable racemization of aspartic acid and phenylalanine should occur during the normal use of aspartame, some food and beverage components could conceivably act as catalysts. Additional studies are required to evaluate whether the use of aspartame as a sugar substitute might not in turn result in an increased human consumption of D-aspartic acid and D-phenylalanine.

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Year:  1984        PMID: 6591191      PMCID: PMC391679          DOI: 10.1073/pnas.81.16.5263

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  10 in total

1.  Decomposition products of L-aspartyl-L-phenylalanine methyl ester and their identification by gas-liquid chromatography.

Authors:  I Furda; P D Malizia; M G Kolor; P J Vernieri
Journal:  J Agric Food Chem       Date:  1975 Mar-Apr       Impact factor: 5.279

2.  Determination of D- and L-amino acids by ion exchange chromatography as L-D and L-L dipeptides.

Authors:  J M Manning; S Moore
Journal:  J Biol Chem       Date:  1968-11-10       Impact factor: 5.157

3.  In vivo racemization in mammalian proteins.

Authors:  J L Bada
Journal:  Methods Enzymol       Date:  1984       Impact factor: 1.600

4.  Sour welcome for aspartame.

Authors:  T Beardsley
Journal:  Nature       Date:  1983 Sep 15-21       Impact factor: 49.962

5.  Aspartame approved despite risks.

Authors:  R J Smith
Journal:  Science       Date:  1981-08-28       Impact factor: 47.728

6.  The stereospecific cyclolization of n-(alpha-hydroxyacyl)-phenylalanyl-proline lactams.

Authors:  H Ott; A J Frey; A Hofmann
Journal:  Tetrahedron       Date:  1963-11       Impact factor: 2.457

7.  Diketopiperazine formation during investigations of amino Acid racemization in dipeptides.

Authors:  S Steinberg; J L Bada
Journal:  Science       Date:  1981-07-31       Impact factor: 47.728

8.  Aspartame--a sweet surprise.

Authors:  R H Mazur
Journal:  J Toxicol Environ Health       Date:  1976-09

Review 9.  Can aspartame meet our expectations?

Authors:  D L Horwitz; J K Bauer-Nehrling
Journal:  J Am Diet Assoc       Date:  1983-08

Review 10.  Food processing and storage as a determinant of protein and amino acid availability.

Authors:  R F Hurrell; P A Finot
Journal:  Experientia Suppl       Date:  1983
  10 in total
  1 in total

1.  The role of carbohydrates at the origin of homochirality in biosystems.

Authors:  Søren Toxvaerd
Journal:  Orig Life Evol Biosph       Date:  2013-08-31       Impact factor: 1.950

  1 in total

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