RESUMEN
It is well-known that a strange flavor, known as off-flavor, might be found in various food products. Even though these substances do not affect our body directly, they can cause a significant change in food flavor and smell, thereby lowering the quality of food products. A well-known example of off-flavor is the transfer of smell from one food product to another. We have previously studied how the smell of limonene, a flavor component of orange juice in paper cartons, is transferred from unopened packages to milk stored in paper cartons, and have confirmed cases where the milk develops a smell completely different from that of limonene. This smell was also confirmed to not have originated from orange juice, and was found to be similar to that of a halogenated phenol. This study aimed to identify this odor component, and our findings indicate the off-flavor component to be 2-iodo-4-methylphenol.
Asunto(s)
Contaminación de Alimentos/análisis , Yodobencenos/análisis , Leche/química , Animales , Análisis de los Alimentos , Odorantes/análisisRESUMEN
Levels of short linear hydroxyproline (Hyp)-containing peptides, such as prolyl-hydroxyproline (Pro-Hyp), increase in human blood after the ingestion of collagen hydrolysate, which has been associated with beneficial effects for human skin and joints. The present study demonstrates the presence of a novel food-derived collagen peptide, cyclic Pro-Hyp, in human blood after the ingestion of collagen hydrolysate. The cyclic Pro-Hyp levels in plasma samples were estimated by liquid chromatography mass spectrometry (LC-MS). Cyclic Pro-Hyp levels significantly increased in the plasma after ingestion of collagen hydrolysate, reaching a maximum level after 2 h and then decreasing. The maximum level of cyclic Pro-Hyp in plasma ranged from 0.1413 to 0.3443 nmol/mL, representing approximately 5% of linear Pro-Hyp in plasma after ingestion of collagen hydrolysate. Addition of cyclic Pro-Hyp in medium at 7 nmol/mL significantly enhanced the growth rate of mouse skin fibroblasts on collagen gel more extensively compared to linear Pro-Hyp.