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固定化果胶酶的合成及其性质研究。

Synthesis and properties of immobilized pectinase onto the macroporous polyacrylamide microspheres.

机构信息

Key Laboratory of Applied Surface and Colloid Chemistry, School of Chemistry and Materials Science, Shaanxi Normal University, Ministry of Education, Xi'an 710062, People's Republic of China.

出版信息

J Agric Food Chem. 2011 Mar 23;59(6):2592-9. doi: 10.1021/jf103719t. Epub 2011 Feb 22.

Abstract

Pectinase was covalently immobilized onto the macroporous polyacrylamide (PAM) microspheres synthesized via an inverse suspension polymerization approach, resulting in 81.7% immobilization yield. The stability of the macroporous PAM support, which has a large surface area, is not impeded by the adsorbed proteins despite the fact that up to 296.3 mg of enzyme is immobilized per gram of the carrier particles. The immobilized enzyme retained more than 75% of its initial activity over 30 days, and the optimum temperature/pH also increased to the range of 50-60 °C/3.0-5.0. The immobilized enzyme also exhibited great operational stability, and more than 75% residual activity was observed after 10 batch reactions. The kinetics of a model reaction catalyzed by the immobilized pectinase was finally investigated. Moreover, the immobilized pectinase could be recovered by centrifuging and showed durable activity at the process of recycle.

摘要

果胶酶通过反相悬浮聚合方法被共价固定在大孔聚丙烯酰胺(PAM)微球上,固定化产率达到 81.7%。尽管每克载体颗粒可以固定多达 296.3 毫克的酶,但具有较大表面积的大孔 PAM 载体的稳定性不会因吸附的蛋白质而受到阻碍。固定化酶在 30 天内保留了超过初始活性的 75%,并且最适温度/ pH 值也增加到 50-60°C/3.0-5.0 范围。固定化酶还表现出出色的操作稳定性,在 10 批反应后观察到超过 75%的残留活性。最后,还研究了固定化果胶酶催化的模型反应的动力学。此外,通过离心可以回收固定化果胶酶,并且在回收过程中显示出持久的活性。

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