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Immobilization of pectinase onto chitosan magnetic nanoparticles by macromolecular cross-linker

机译:大分子交联剂将果胶酶固定到壳聚糖磁性纳米粒子上

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摘要

Pectinase was immobilized onto chitosan magnetic nanoparticles (CMNPs) by dextran polyaldehyde as a macromolecular cross-linking agent. The parameters like cross-linking concentration, time and CMNPs to enzyme ratio were optimized. Further, prepared magnetic pectinase nanobiocatalyst was characterized by FT-IR and XRD. The thermal kinetic studies for immobilized pectinase showed two folds improved thermal stability in the range of 55-75 degrees C as compared to free form. The V-max and K-m values of immobilized pectinase were found to be nearly equal to native form which indicated that conformational flexibility of pectinase was retained even after immobilization. The residual activity of immobilized pectinase was 85% after seven successive cycles of reuse, while it retained upto 89% residual activity on storage of fifteen days which exhibited excellent stability and durability. The conformational changes in pectinase after immobilization were evaluated by FT-IR spectroscopy data analysis tools. Finally, magnetic pectinase nanobiocatalyst was employed for apple juice clarification which showed turbidity reduction upto 74% after 150 min treatment. (C) 2016 Elsevier Ltd. All rights reserved.
机译:用葡聚糖聚醛作为大分子交联剂将果胶酶固定在壳聚糖磁性纳米颗粒(CMNP)上。优化了交联浓度,时间和CMNP的参数,得到酶比。此外,制备的磁性果胶酶纳米双催化剂的特征在于FT-IR和XRD。与游离形式相比,固定化果胶酶的热动力动力学研究表明,两倍改善了55-75℃的热稳定性。发现固定化果胶酶的V-MAX和K-M值几乎等于天然形式,这表明即使在固定后均匀地保留果胶酶的柔韧性。在七个连续再利用循环后,固定化果胶酶的残余活性为85%,而其在十五天内保留高达89%的残余活性,这表现出优异的稳定性和耐用性。通过FT-IR光谱数据分析工具评估固定后果胶酶的构象变化。最后,磁性果胶酶纳米双胆催化剂用于苹果汁澄清,在150分钟处理后显示出浊度降低74%。 (c)2016 Elsevier Ltd.保留所有权利。

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