Unknown

Dataset Information

0

Simulated Sunlight Selectively Modifies Maillard Reaction Products in a Wide Array of Chemical Reactions.


ABSTRACT: The photochemical transformation of Maillard reaction products (MRPs) under simulated sunlight into mostly unexplored photoproducts is reported herein. Non-enzymatic glycation of amino acids leads to a heterogeneous class of intermediates with extreme chemical diversity, which is of particular relevance in processed and stored food products as well as in diabetic and age-related protein damage. Here, three amino acids (lysine, arginine, and histidine) were reacted with ribose at 100?°C in water for ten hours. Exposing these model systems to simulated sunlight led to a fast decay of MRPs. The photodegradation of MRPs and the formation of new compounds have been studied by fluorescence spectroscopy and nontargeted (ultra)high-resolution mass spectrometry. Photoreactions showed strong selectivity towards the degradation of electron-rich aromatic heterocycles, such as pyrroles and pyrimidines. The data show that oxidative cleavage mechanisms dominate the formation of photoproducts. The photochemical transformations differed fundamentally from "traditional" thermal Maillard reactions and indicated a high amino acid specificity.

SUBMITTER: Hemmler D 

PROVIDER: S-EPMC6856810 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Simulated Sunlight Selectively Modifies Maillard Reaction Products in a Wide Array of Chemical Reactions.

Hemmler Daniel D   Gonsior Michael M   Powers Leanne C LC   Marshall James W JW   Rychlik Michael M   Taylor Andrew J AJ   Schmitt-Kopplin Philippe P  

Chemistry (Weinheim an der Bergstrasse, Germany) 20190913 57


The photochemical transformation of Maillard reaction products (MRPs) under simulated sunlight into mostly unexplored photoproducts is reported herein. Non-enzymatic glycation of amino acids leads to a heterogeneous class of intermediates with extreme chemical diversity, which is of particular relevance in processed and stored food products as well as in diabetic and age-related protein damage. Here, three amino acids (lysine, arginine, and histidine) were reacted with ribose at 100 °C in water  ...[more]

Similar Datasets

| S-EPMC5468300 | biostudies-literature
2009-12-25 | GSE18950 | GEO
2010-05-16 | E-GEOD-18950 | biostudies-arrayexpress
| S-EPMC4779479 | biostudies-literature
| S-EPMC5785397 | biostudies-literature
| S-EPMC10616461 | biostudies-literature
| S-EPMC6146089 | biostudies-literature
| S-EPMC1221264 | biostudies-other
| S-EPMC3915869 | biostudies-literature
| S-EPMC9562662 | biostudies-literature