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https://ir.cnu.edu.tw/handle/310902800/34543
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| 標題: | Novel Glycosylation by Amylosucrase to Produce Glycoside Anomers |
| 作者: | Wu, Jiumn-Yih
Ding, Hsiou-Yu
Luo, Shun-Yuan
Wang, Tzi-Yuan
Tsai, Yu-Li
Chang, Te-Sheng |
| 貢獻者: | Chia Nan University of Pharmacy & Science
National Chung Hsing University
Academia Sinica - Taiwan
National University Tainan |
| 關鍵字: | ganoderic acid g
triterpenoids
lucidum |
| 日期: | 2022 |
| 上傳時間: | 2023-12-11 13:57:02 (UTC+8) |
| 出版者: | MDPI |
| 摘要: | Simple Summary All livings are composed of cells, which contain lipid, proteins, nuclei acids, and saccharides. Saccharides include polysaccharides, oligo saccharides, disaccharides, which are linked by monosaccharides. Monosaccharides such as glucose exist in two forms, named alpha and beta anomer, in solution. In addition, monosaccharides could be linked with lipid, proteins, nuclei acids or other saccharide to form glycosides through glycosylation. In nature, glycosylation is catalyzed by enzymes. Until now, all enzymes catalyzed glycosylation to form glycosides with either alpha or beta form but not both. This study found an enzyme, amylosucrase from Deinococcus geothermalis (DgAS), could catalyze glycosylation of a kind of lipid named ganoderic acids triterpenoids from a medicinal fungus Ganoderma lucidum to form both alpha and beta anomer of glycosides. This is the first report that enzymes could catalyze such glycosylation and a possible reaction mechanism was proposed. Glycosylation occurring at either lipids, proteins, or sugars plays important roles in many biological systems. In nature, enzymatic glycosylation is the formation of a glycosidic bond between the anomeric carbon of the donor sugar and the functional group of the sugar acceptor. This study found novel glycoside anomers without an anomeric carbon linkage of the sugar donor. A glycoside hydrolase (GH) enzyme, amylosucrase from Deinococcus geothermalis (DgAS), was evaluated to glycosylate ganoderic acid F (GAF), a lanostane triterpenoid from medicinal fungus Ganoderma lucidum, at different pH levels. The results showed that GAF was glycosylated by DgAS at acidic conditions pH 5 and pH 6, whereas the activity dramatically decreased to be undetectable at pH 7 or pH 8. The biotransformation product was purified by preparative high-performance liquid chromatography and identified as unusual alpha-glucosyl-(2 -> 26)-GAF and beta-glucosyl-(2 -> 26)-GAF anomers by mass and nucleic magnetic resonance (NMR) spectroscopy. We further used DgAS to catalyze another six triterpenoids. Under the acidic conditions, two of six compounds, ganoderic acid A (GAA) and ganoderic acid G (GAG), could be converted to alpha-glucosyl-(2 -> 26)-GAA and beta-glucosyl-(2 -> 26)-GAA anomers and alpha-glucosyl-(2 -> 26)-GAG and beta-glucosyl-(2 -> 26)-GAG anomers, respectively. The glycosylation of triterpenoid aglycones was first confirmed to be converted via a GH enzyme, DgAS. The novel enzymatic glycosylation-formed glycoside anomers opens a new bioreaction in the pharmaceutical industry and in the biotechnology sector. |
| 關聯: | BIOLOGY-BASEL, v.11, n.CB2, pp.CC2, pp.-, |
| 顯示於類別: | [行政單位] 123
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