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Optimum chalcone synthase for flavonoid biosynthesis in microorganisms.
Tong, Yingjia; Lyu, Yunbin; Xu, Sha; Zhang, Liang; Zhou, Jingwen.
Affiliation
  • Tong Y; National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi, China.
  • Lyu Y; Key Laboratory of Industrial Biotechnology, Ministry of Education and School of Biotechnology, Jiangnan University, Wuxi, China.
  • Xu S; Science Center for Future Foods, School of Biotechnology, Jiangnan University, Wuxi, China.
  • Zhang L; National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi, China.
  • Zhou J; Key Laboratory of Industrial Biotechnology, Ministry of Education and School of Biotechnology, Jiangnan University, Wuxi, China.
Crit Rev Biotechnol ; 41(8): 1194-1208, 2021 Dec.
Article in En | MEDLINE | ID: mdl-33980085
Chalcones and the subsequently generated flavonoids, as well as flavonoid derivatives, have been proven to have a variety of physiological activities and are widely used in: the pharmaceutical, food, feed, and cosmetic industries. As the content of chalcones and downstream products in native plants is low, the production of these compounds by microorganisms has gained the attention of many researchers and has a history of more than 20 years. The mining and engineering of chalcone synthase (CHS) could be one of the most important ways to achieve more efficient production of chalcones and downstream products in microorganisms. CHS has a broad spectrum of substrates, and its enzyme activity and expression level can significantly affect the efficiency of the biosynthesis of flavonoids. This review summarizes the recent advances in the: structure, mechanism, evolution, substrate spectrum, transformation, and expression regulation in the flavonoid biosynthesis of this vital enzyme. Future development directions were also suggested. The findings may further promote the research and development of flavonoids and health products, making them vital in the fields of human diet and health.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Flavonoids / Acyltransferases Limits: Humans Language: En Journal: Crit Rev Biotechnol Journal subject: BIOTECNOLOGIA Year: 2021 Document type: Article Affiliation country: China Country of publication: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Flavonoids / Acyltransferases Limits: Humans Language: En Journal: Crit Rev Biotechnol Journal subject: BIOTECNOLOGIA Year: 2021 Document type: Article Affiliation country: China Country of publication: United kingdom