Kinetics of Interaction of Vanillin with Amino Acids and Peptides in Model Systems
| Autor: | I.J. Jeon, J. S. Smith, Chobpattana W |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
chemistry.chemical_classification
Chromatography Aspartame Vanillin Kinetics Phenylalanine General Chemistry Amino acid Chemical kinetics Maillard reaction symbols.namesake chemistry.chemical_compound Reaction rate constant Models Chemical chemistry Benzaldehydes symbols Organic chemistry Amino Acids Peptides General Agricultural and Biological Sciences |
| Zdroj: | Journal of Agricultural and Food Chemistry. 48:3885-3889 |
| ISSN: | 1520-5118 0021-8561 |
| DOI: | 10.1021/jf9912102 |
| Popis: | Model systems were used to study the reaction kinetics of vanillin and pentalysine, lysine, glutathione, cysteine, aspartame, or phenylalanine (molar ratio 1:1) in phosphate buffer. The buffer pH was adjusted to the pKa2 of the available α-amino group of each amino acid or peptide. Reductions of vanillin followed first-order kinetics at 55, 65, and 75 °C in the presence of each of the amino acids or peptides used. The reaction rates were accelerated as the temperature increased. The rate constants were highest for pentalysine followed by lysine, phenylalanine, glutathione/cysteine, and aspartame. The reduction of phenylalanine followed first-order kinetics, whereas the formation of its reaction product followed zero-order kinetics. The activation energy (Ea) for the reaction ranged from 5.6 to 14.5 kcal/mol. Keywords: Vanillin; kinetics order; amino acids; peptides; flavor |
| Databáze: | OpenAIRE |
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