Voronezh State University, Russia.
Kazan Federal University, Russia.
Int J Biol Macromol. 2018 Aug;115:829-834. doi: 10.1016/j.ijbiomac.2018.04.107. Epub 2018 Apr 23.
The enzymatic hydrolysis of poly- and oligosaccharides from plants seems like an advantageous approach for sugars production. Two inulinases producing fructose from plant oligosaccharides were isolated from yeast Kluyveromyces marxianus and plant Helianthus tuberosus. Both enzymes were immobilized on polymeric carriers by using the static adsorption approach. We could save 80.4% of the initial catalytic activity of plant inulinase immobilized on KU-2 cation-exchange resin and 75.5% of yeast enzyme activity adsorbed on AV-17-2P anion-exchange resin. After immobilization, the Km values increased 1.5 and 6 times for enzymes from K. marxianus and H. tuberosus, respectively. The optimal temperatures for catalysis of both enzymes were increased from 48-50 °C up to 70 °C. The activities of both immobilized enzymes remained unchanged after the 10 cycles of 20-min hydrolysis reaction at 70 °C model batch reactor. Sorbents, native and immobilized enzymes did not exhibit any mutagenic or cytotoxic activity.
从植物中提取多糖和寡糖的酶解似乎是一种生产糖的有利方法。从酵母 Kluyveromyces marxianus 和植物菊芋中分离到两种能够从植物寡糖中产生果糖的菊粉酶。这两种酶都通过静态吸附法固定在聚合物载体上。我们可以分别保存 KU-2 阳离子交换树脂固定化植物菊粉酶和 AV-17-2P 阴离子交换树脂吸附酵母酶初始催化活性的 80.4%和 75.5%。固定化后，Km 值分别增加了 1.5 倍和 6 倍，来自 K. marxianus 和 H. tuberosus 的酶。两种酶的最适催化温度均从 48-50°C 升高至 70°C。在 70°C 模型分批反应器中进行 10 次 20 分钟水解反应循环后，两种固定化酶的活性均保持不变。吸附剂、天然酶和固定化酶均未表现出任何诱变或细胞毒性活性。
