کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4752748 | 1416368 | 2017 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Synthesis and characterization of novel astragalin galactosides using β-galactosidase from Bacillus circulans Synthesis and characterization of novel astragalin galactosides using β-galactosidase from Bacillus circulans](/preview/png/4752748.png)
- Novel astragalin-galactosides were synthesized using β-galactosidase and lactose.
- Response surface method was used to optimize astragalin conversion yields.
- Chemical structures of novel Ast-Gals were determined by NMR.
- Water solubility of Ast-Gal2 was 1500 fold higher compared to astragalin.
- Ast-Gals retained the antioxidant and ACE inhibitory activities of Ast.
Astragalin (kaempferol-3-O-β-d-glucopyranoside, Ast) is a kind of flavonoid known to have anti-oxidant, anti-HIV, anti-allergic, and anti-inflammatory effects. It has low solubility in water. In this study, novel astragalin galactosides (Ast-Gals) were synthesized using β-galactosidase from Bacillus circulans and reaction conditions were optimized to increase the conversion yield of astragallin. Purified Ast-Gal1 (11.6% of Ast used, w/w) and Ast-Gal2 (6.7% of Ast used, w/w) were obtained by medium pressure chromatography (MPLC) with silica C18 column and open column packed with Sephadex LH-20. The structures of Ast-Gal1 and Ast-Gal2 were identified by nuclear magnetic resonance (NMR) to be kaempferol-3-O-β-d-glucopyranosyl-(1 â 6)-β-d-galactopyranoside and kaempferol-3-O-β-d-glucopyranosyl-(1 â 6)-β-d-galactopyranosyl-(1 â 4)-β-d-galactopyranoside, respectively. The water solubility of Ast, Ast-Gal1, and Ast-Gal2 were 28.2 ± 1.2 mg/L, 38,300 ± 3.5 mg/L, and 38,800 ± 2.8 mg/L, respectively. The SC50 value (the concentration required to scavenge 50% of the ABTS+ ) of Ast, Ast-Gal1, and Ast-Gal2 were 5.1 ± 1.6 μM, 6.5 ± 0.4 μM, and 4.9 ± 1.1 μM, respectively. The IC50 values (the half maximal inhibitory concentration) of Ast, Ast-Gal1, and Ast-Gal2 against angiotensin converting enzyme (ACE) were 171.0 ± 1.2 μM, 186.0 μM, and 139.0 ± 0.2 μM, respectively.
170
Journal: Enzyme and Microbial Technology - Volume 103, August 2017, Pages 59-67