期刊
MOLECULES
卷 26, 期 20, 页码 -出版社
MDPI
DOI: 10.3390/molecules26206274
关键词
glycoside hydrolase; glycosyltransferase; glycosylation; vitexin; glucoside
资金
- Ministry of Science and Technology of Taiwan [MOST 110-2221-E-024-002, MOST 110-2221-E-507-002]
Researchers found that an enzyme from Bacillus thuringiensis could convert vitexin into two new compounds with higher aqueous solubility, which enhances the potential applications of vitexin.
Vitexin is a C-glucoside flavone that exhibits a wide range of pharmaceutical activities. However, the poor solubility of vitexin limits its applications. To resolve this limitation, two glycoside hydrolases (GHs) and four glycosyltransferases (GTs) were assayed for glycosylation activity toward vitexin. The results showed that BtGT_16345 from the Bacillus thuringiensis GA A07 strain possessed the highest glycosylation activity, catalyzing the conversion of vitexin into new compounds, vitexin-4 '-O-beta-glucoside (1) and vitexin-5-O-beta-glucoside (2), which showed greater aqueous solubility than vitexin. To our knowledge, this is the first report of vitexin glycosylation. Based on the multiple bioactivities of vitexin, the two highly soluble vitexin derivatives might have high potential for pharmacological usage in the future.
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