Radical-assisted melanoidin formation during thermal processing of foods as well as under physiological conditions |
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| Authors: | Hofmann T Bors W Stettmaier K |
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| Institution: | Deutsche Forschungsanstalt für Lebensmittelchemie, Lichtenbergstrasse 4, D-85748 Garching, Germany. hofmann@dfa.leb.chemie.tu-muenchen.de |
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| Abstract: | Color-generating reactions of protein-bound lysine with carbohydrates were studied under thermal as well as under physiological conditions to gain insights into the role of protein/carbohydrate reactions in the formation of food melanoidins as well as nonenzymatic browning products in vivo. EPR spectroscopy of orange-brown melanoidins, which were isolated from heated aqueous solutions of bovine serum albumin and glycolaldehyde, revealed the protein-bound 1,4-bis(5-amino-5-carboxy-1-pentyl)pyrazinium radical cation (CROSSPY) as a previously unknown type of cross-linking amino acid leading to protein dimerization. To verify their formation in foods, wheat bread crust and roasted cocoa as well as coffee beans, showing elevated nonenzymatic browning, were investigated by EPR spectroscopy. An intense radical was detected, which, by comparison with the radical formed upon reaction bovine serum albumin with glycolaldehyde, was identified as the protein-bound CROSSPY. The radical-assisted protein oligomerization as well as the browning of bovine serum albumin in the presence of glycolaldehyde occurred also rapidly under physiological conditions, thereby suggesting CROSSPY formation to be probably involved also in nonenzymatic glycation reactions in vivo. |
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