Proteins or amino acids are subjected to the Maillard (browning) reaction in the presence of reducing sugars and catalyzed by high temperature. The reaction occurs in daily-life cooking and in the human body. Although the reaction is ubiquitous and has been known for over 100 years, it still intrigues researchers across disciplines. Here we report an unexpected finding where proteins and amino acids turn brown in a mixture of two common solvents: dimethyl sulfoxide and acetone. The browning reaction proceeds at room temperature, without the presence of any sugars. This novel browning reaction was confirmed by a series of investigation on a protein-based gel, 3 proteins and 20 amino acids. The browning is spontaneous, regardless of whether the protein or amino acid was dissolved or not. The kinetic study reveals a fast reaction with a formation half-life of about 4 h. Notably, the reactivity is bell-shaped, with the maximal catalytic effect occurring at an acetone-to-DMSO volume ratio of 0.1–0.3. Among the 20 amino acids tested, tryptophan, lysine, and proline are the most susceptible amino acids to the solvent-mediated browning reaction.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - 15 Jan 2021|
- Amino acids
- Browning reaction
- Maillard reaction