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通过高分子交联剂将果胶酶固定在壳聚糖磁性纳米颗粒上。

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

机构信息

Department of Chemical Engineering, Institute of Chemical Technology, Matunga (E), Mumbai 400019, India.

Department of Chemical Engineering, Institute of Chemical Technology, Matunga (E), Mumbai 400019, India.

出版信息

Carbohydr Polym. 2017 Feb 10;157:677-685. doi: 10.1016/j.carbpol.2016.10.018. Epub 2016 Oct 8.


DOI:10.1016/j.carbpol.2016.10.018
PMID:27987978
Abstract

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°C as compared to free form. The V and K 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 150min treatment.

摘要

果胶酶通过葡聚糖多醛作为高分子交联剂固定在壳聚糖磁性纳米颗粒(CMNPs)上。优化了交联浓度、时间和 CMNPs 与酶的比例等参数。进一步,通过傅里叶变换红外光谱(FT-IR)和 X 射线衍射(XRD)对制备的磁性果胶酶纳米生物催化剂进行了表征。与游离形式相比,固定化果胶酶的热动力学研究表明,在 55-75°C 的范围内,其热稳定性提高了两倍。固定化果胶酶的 V 和 K 值接近天然形式,这表明即使在固定化后,果胶酶的构象灵活性也得以保留。固定化果胶酶在连续重复使用七次后,其残余活性仍保持在 85%,在储存 15 天内仍保留 89%的残余活性,表现出优异的稳定性和耐用性。通过傅里叶变换红外光谱数据分析工具评估了固定化后果胶酶的构象变化。最后,将磁性果胶酶纳米生物催化剂用于苹果汁澄清,在 150min 处理后,浊度降低了 74%。

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