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首页> 外文期刊>Romanian Biotechnology Letters >Hydrolysis of galacto-oligosaccharides in soymilk by immobilized α-galactosidase from Chaetomium madarasense AUMC 9376
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Hydrolysis of galacto-oligosaccharides in soymilk by immobilized α-galactosidase from Chaetomium madarasense AUMC 9376

机译:固定化madarasense拟南芥AUMC 9376中的α-半乳糖苷酶水解豆浆中的半乳糖低聚糖

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摘要

a-galactosidase 3.2.1.22 (a-Gal) enzyme was produced from Chaetomium madarasense AUMC 9376 under solid state fermentation using banana peels as substrate. Optimal a—Gal production was obtained at initial pH 5 and, 40°C then the enzyme was completely purified resulting in 25.32 folds purification (1561.67 U/mg). The enzyme was immobilized in technical grade sodium alginate and gelatin. The characteristics of the free and immobilized enzyme were also investigated. The optimum temperature for both enzymes was 50°C and 60°C, respectively, while, the optimum pH for both was 5. Besides, the pH stability and thermal stability of the free and immobilized enzyme were also studied. Immobilized a—Gal was more stable at high pH and temperatures than the soluble one. The results showed that the catalytic properties of the immobilized enzyme were improved. Moreover, HPLC chromatograms revealed that the immobilized enzyme has the ability to reduce raffinose and stachyose oligosaccharides in soymilk by 69.2 and 64.3%, respectively.
机译:α-半乳糖苷酶3.2.1.22(α-Gal)酶是使用香蕉皮作为底物在固态发酵下由Chaetomium madarasense AUMC 9376生产的。在初始pH 5和40°C时可获得最佳的α-Gal产量,然后将酶完全纯化,从而得到25.32倍的纯化率(1561.67 U / mg)。将该酶固定在工业级海藻酸钠和明胶中。还研究了游离和固定化酶的特性。两种酶的最佳温度分别为50℃和60℃,而两种酶的最佳pH均为5。此外,还研究了游离和固定化酶的pH稳定性和热稳定性。固定化的α-Gal在高pH和高温下比可溶的α-Gal更稳定。结果表明,固定化酶的催化性能得到改善。此外,HPLC色谱图表明,固定化酶具有将豆浆中的棉子糖和水苏糖寡糖分别降低69.2%和64.3%的能力。

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