Department of Biotechnology, University Institute of Engineering Technology, Panjab University, Chandigarh, India.
Department of Medical Laboratory Sciences, Lovely Professional University, Phagwara 144411, Punjab, India.
Int J Biol Macromol. 2020 Aug 1;156:1347-1358. doi: 10.1016/j.ijbiomac.2019.11.175. Epub 2019 Nov 23.
Partially purified β-mannanase was immobilized on the modified matrix of sodium alginate-grafted-β-cyclodextrin. The Fourier-transform infrared spectroscopy (FTIR) and X-ray diffraction characterization proved that β-cyclodextrin (β-CD) was successfully grafted with sodium alginate. After successful immobilization, yield of enzyme was found 91.5%, pH and temperature optima were increased, 6.0 to 7.0 and 50 °C to 55 °C respectively. Immobilized mannanase was able to reuse 15 times and retained its 70% activity, meanwhile the immobilized enzyme showed 60% activity after 30 days of storage at 4 °C. Immobilization also increased the thermostability and half-life of the enzyme when compared to the free mannanase. During the comparison of adsorption isotherm and kinetic models, Langmuir isotherm and pseudo-first order kinetics were observed to be the best fit model for the confirmation of immobilization.
部分纯化的β-甘露聚糖酶被固定在经过修饰的海藻酸钠接枝-β-环糊精基质上。傅里叶变换红外光谱(FTIR)和 X 射线衍射表征证明β-环糊精(β-CD)已成功接枝到海藻酸钠上。成功固定化后,酶的产率为 91.5%,pH 和温度最适值分别提高到 6.0 到 7.0 和 50°C 到 55°C。固定化甘露聚糖酶可重复使用 15 次,保持 70%的活性,同时,在 4°C 下储存 30 天后,固定化酶仍保留 60%的活性。与游离甘露聚糖酶相比,固定化还提高了酶的热稳定性和半衰期。在吸附等温线和动力学模型的比较中,观察到 Langmuir 等温线和拟一级动力学是用于确认固定化的最佳拟合模型。