• Food Science of Animal Resources
• /
• v.32 no.5
• /
• pp.540-544
• /
• 2012

During heat treatment and storage of milk, deteriorative reaction takes place, which consequently influence on the milk quality. In this study, formation of lactulose and furosine under different thermal conditions and storage conditions, and the ratio of lactulose and furosine (LU/FU) in presence of reconstituted milk powder were determined to establish chemical indicators for heat damages of milk and the adulteration of fresh milk in dairy field. The lactulose and furosine contents linearly increased with increased heating temperature and heating time. It showed high correlation between the formation of lactulose and furosine, and the treatment temperature and time (p<0.05). The lactulose and furosine concentration of HTST milk and UHT milk noticeably increased during storage at $30^{\circ}C$, but there was no noticeable increase of lactulose and furosine concentration at lower storage temperature. In the raw milk, the lactulose and furosine contents greatly increased with the addition of reconstituted milk. The increase level of furosine was much higher than that of lactulose, which consequently resulted in the lower LU/FU ratio in milk as increase of added reconstituted milk amounts. As comparing with raw milk, there was more than twice reduction in LU/FU ratios after the addition of reconstituted milk (p<0.05). It can be concluded that lactulose and furosine are suitable milk quality indicators of heat damage and for demonstrating improper addition of reconstituted milk powder.

• Journal of Ginseng Research
• /
• v.42 no.1
• /
• pp.21-26
• /
• 2018

Background: Furosine (${\varepsilon}$-N-2-furoylmethyl-L-lysine, FML) is an amino acid derivative, which is considered to be an important indicator of the extent of damage (deteriorating the quality of amino acid and proteins due to a blockage of lysine and a decrease in the digestibility of proteins) during the early stages of the Maillard reaction. In addition, FML has been proven to be harmful because it is closely related to a variety of diseases such as diabetes. The qualitative analysis of FML in fresh and processed ginsengs was confirmed using HPLC-MS. Methods: An ion-pair reversed-phase LC method was used for the quantitative analysis of FML in various ginseng samples. Results: The contents of FML in the ginseng samples were 3.35-42.28 g/kg protein. The lowest value was observed in the freshly collected ginseng samples, and the highest value was found in the black ginseng concentrate. Heat treatment and honey addition significantly increased the FML content from 3.35 g/kg protein to 42.28 g/kg protein. Conclusion: These results indicate that FML is a promising indicator to estimate the heat treatment degree and honey addition level during the manufacture of ginseng products. The FML content is also an important parameter to identity the quality of ginseng products. In addition, the generation and regulation of potentially harmful Maillard reaction products-FML in ginseng processing was also investigated, providing a solid theoretical foundation and valuable reference for safe ginseng processing.

• Food Science and Biotechnology
• /
• v.15 no.4
• /
• pp.617-624
• /
• 2006

Various plant phenolics were assessed for (${\beta}$-secretase (BACE1) inhibitory activity in order to screen for anti-dementia agents. Among 39 phenolics, eight compounds, 1,2,3-trigalloyl glucopyranoside, acetonyl geraniin, euphorscopin, furosine, helioscopinin A, helioscopinin B, jolkinin, and rugosin E exhibited strong inhibition of BACE1 with $IC_{50}$ values of $5.87{\times}10^{-8}-54.93{\times}10^{-6}\;M$. Among them, rugosin E was the most potent ($IC_{50}$ $5.87{\times}10^{-8}\;M$). The active compounds were shown to be non-competitive inhibitors by Dixon plot. All the phenolic BACE1 inhibitors except furosin also suppressed prolyl endopeptidase (PEP) activity. However, these phenolic compounds caused less inhibition of ${\alpha}$-secretase (tumor necrosis factor a converting enzyme; TACE) and no significant inhibition of other serine proteases such as trypsin, chymotrypsin, and elastase was seen, demonstrating that they are relatively specific to both BACE1 and PEP. No significant structure-activity relationships were found.