Your browser doesn't support javascript.
loading
Bitterness quantification and simulated taste mechanism of theasinensin A from tea.
Zhang, Jian-Yong; Cui, Hong-Chun; Feng, Zhi-Hui; Wang, Wei-Wei; Zhao, Yun; Deng, Yu-Liang; Jiang, He-Yuan; Yin, Jun-Feng; Engelhardt, Ulrich H.
Afiliação
  • Zhang JY; Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou, China.
  • Cui HC; Tea Research Institute of Hangzhou Academy of Agricultural Science, Hangzhou, China.
  • Feng ZH; Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou, China.
  • Wang WW; Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou, China.
  • Zhao Y; Tea Research Institute of Hangzhou Academy of Agricultural Science, Hangzhou, China.
  • Deng YL; Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou, China.
  • Jiang HY; Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou, China.
  • Yin JF; Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou, China.
  • Engelhardt UH; Institute of Food Chemistry, Brunswick University of Technology, Braunschweig, Germany.
Front Nutr ; 10: 1138023, 2023.
Article em En | MEDLINE | ID: mdl-37229471
Theasinensin A is an important quality chemical component in tea, but its taste characteristics and the related mechanism are still unclear. The bitterness quantification and simulated taste mechanism of theasinensin A were researched. The results showed that theasinensin A was significantly correlated with the bitterness of tea. The bitterness threshold of theasinensin A was identified as 65 µmol/L for the first time. The dose-over-threshold (DOT) value of theasinensin A was significantly higher than that of caffeine in black tea soup. The concentration-bitterness curve and time-intensity curve of theasinensin A were constructed. The bitterness contribution of theasinensin A in black tea was higher than in oolong and green tea. Theasinensin A had the highest affinity with bitterness receptor protein TAS2R16, which was compared to TAS2R13 and TAS2R14. Theasinensin A was mainly bound to a half-open cavity at the N-terminal of TAS2R13, TAS2R14, and TAS2R16. The different binding capacity, hydrogen bond, and hydrophobic accumulation effect of theasinensin A and bitterness receptor proteins might be the reason why theasinensin A presented different bitterness senses in human oral cavity.
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Tipo de estudo: Prognostic_studies Idioma: En Revista: Front Nutr Ano de publicação: 2023 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Tipo de estudo: Prognostic_studies Idioma: En Revista: Front Nutr Ano de publicação: 2023 Tipo de documento: Article País de afiliação: China
...