Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, P.O. Box 14155-6451, Tehran, 1417614411, Iran; Department of Pharmaceutical Biotechnology, School of Pharmacy, Zanjan University of Medical Sciences, Zanjan, Iran.
Department of Pharmaceutical Biotechnology, School of Pharmacy, Zanjan University of Medical Sciences, Zanjan, Iran.
Carbohydr Res. 2019 Sep 1;483:107746. doi: 10.1016/j.carres.2019.107746. Epub 2019 Jul 13.
Bacterial inulinases are the key enzymes in the enzymatic hydrolysis of inulin and production of fructooligosaccharides (FOSs) and high fructose syrup (HFS). An extremophilic inulinase was purified from Alkalibacillus filiformis using 80% ethanol precipitation, ultrafiltration, and Q-Sepharose anion exchange chromatography. The purified inulinase was highly active in a wide range of pH, temperature, chemical reagents, and NaCl concentrations. The enzyme immobilization on cobalt ferrite magnetic nanoparticles (CoFeO MNPs) was carried out by carrier binding method with covalent linkage and showed improved stability and reusability within a broad temperature and pH range, compared with the free enzyme. Using free and immobilized inulinases from A. filiformis, 122 g L and 160 g L fructose with 61% and 80% conversion, respectively, were obtained, with inulin as the substrate. The enzymatic properties, such as notable stability under extreme conditions, make the inulinase from A. filiformis a promising candidate for related biotechnological applications.
细菌菊粉酶是酶解菊粉生产果寡糖（FOS）和高果糖浆（HFS）的关键酶。本文从丝状嗜碱杆菌中纯化了一种极端耐热的菊粉酶，采用 80%乙醇沉淀、超滤和 Q-琼脂糖阴离子交换层析进行纯化。该菊粉酶在较宽的 pH 值、温度、化学试剂和 NaCl 浓度范围内具有很高的活性。通过载体结合法，用共价键将酶固定在钴铁氧体磁性纳米粒子（CoFeO MNPs）上，与游离酶相比，该固定化酶在较宽的温度和 pH 范围内显示出更好的稳定性和可重复使用性。用来自丝状嗜碱杆菌的游离和固定化菊粉酶，以菊粉为底物，分别获得 122 g/L 和 160 g/L 的果糖，转化率分别为 61%和 80%。该菊粉酶在极端条件下具有显著的稳定性等酶学性质，使其成为相关生物技术应用的有前途的候选酶。
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