19746-33-9Relevant articles and documents
Studies on N-terminal glycation of peptides in hypoallergenic infant formulas: Quantification of α-N-(2-furoylmethyl) amino acids
Penndorf, Ilka,Biedermann, Daniela,Maurer, Sarah V.,Henle, Thomas
, p. 723 - 727 (2007)
To obtain information about the extent of the early Maillard reaction between the N-termini of peptides and lactose, α-N-(2-furoylmethyl) amino acids (FMAAs) were quantified together with ε-A/-(2-furoylmethyl)lysine (furosine) in acid hydrolyzates of hypoallergenic infant formulas, conventional infant formulas, and human milk samples using RP-HPLC with UV-detection. FMAAs are formed during acid hydrolysis of peptide-bound N-terminal Amadori products (APs), and furosine is formed from the Amadori products of peptide-bound lysine. Unambiguous identification was achieved by means of LC/MS and UV-spectroscopy using independently prepared reference material. The extent of acid-induced conversion of APs to FMAAs was studied by RP-HPLC with chemiluminescent nitrogen detection (CLND). Depending on the corresponding a-A/-lactulosyl amino acid, between 6.0% and 18.1% of FMAAs were formed during hydrolysis for 23 h at 110 °C in 8 N HCl. From espi;-N-lactulosyllysine, 50% furosine is formed under these conditions. Whereas furosine was detectable in all assayed samples, five different FMAAs, α-FM-Lys, α-FM-Ala, α-FM-Val, α-FM-lle, and α-FM-Leu, were exclusively detected in acid hydrolyzates of hypoallergenic infant formulas in amounts ranging from 35 to 396 μmol/100 g protein. Taking the conversion factors into account, modification of N-terminal amino acids in peptides by reducing carbohydrates was between 0.3% and 8.4%. This has to be considered within the discussion concerning the nutritional quality of peptide-containing foods.
Finot et al.
, p. 1097 (1968)