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Recent Progress in Physiological Significance and Biosynthesis of Lacto-N-triose II: Insights into a Crucial Biomolecule.
Guang, Cuie; Du, Zhihui; Meng, Jiawei; Zhu, Yunqi; Zhu, Yingying; Mu, Wanmeng.
Affiliation
  • Guang C; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.
  • Du Z; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.
  • Meng J; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.
  • Zhu Y; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.
  • Zhu Y; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.
  • Mu W; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.
J Agric Food Chem ; 72(36): 19539-19548, 2024 Sep 11.
Article in En | MEDLINE | ID: mdl-39188079
ABSTRACT
Lacto-N-triose II (LNTri II), an important precursor for human milk oligosaccharide (HMOs) synthesis, has garnered significant attention due to its structural features and physiological properties. Composed of galactose (Gal), N-acetylglucosamine (GlcNAc), and glucose (Glc), with the chemical structure GlcNAcß1,3Galß1,4Glc, the distinctive structure of LNTri II confers various physiological functions such as promoting the growth of beneficial bacteria, regulating the infant immune system, and preventing certain gastrointestinal diseases. Extensive research efforts have been dedicated to elucidating efficient enzymatic synthesis pathways for LNTri II production, with particular emphasis on the transglycosylation activity of ß-N-acetylhexosaminidases and the action of ß-1,3-N-acetylglucosaminyltransferases. Additionally, metabolic engineering and cell factory approaches have been explored, harnessing the potential of engineered microbial hosts for the large-scale biosynthesis of LNTri II. This review summarizes the structure, derivatives, physiological effects, and biosynthesis of LNTri II.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacteria Limits: Animals / Humans Language: En Journal: J Agric Food Chem / J. agric. Food chem / Journal of agricultural and food chemistry Year: 2024 Document type: Article Country of publication: Estados Unidos

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacteria Limits: Animals / Humans Language: En Journal: J Agric Food Chem / J. agric. Food chem / Journal of agricultural and food chemistry Year: 2024 Document type: Article Country of publication: Estados Unidos