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首页> 外文期刊>RSC Advances >A novel strategy to immobilize enzymes on microporous membranes via dicarboxylic acid halides
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A novel strategy to immobilize enzymes on microporous membranes via dicarboxylic acid halides

机译：通过二羧酸卤化物 将酶固定在微孔膜上的新策略

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A major challenge in enhancing the acceptability of enzymes in enzymatic membrane bioreactors (EMBRs) for industrial processes lies in effectively immobilizing enzymes on supports while maintaining their conformation and activity. This work describes a novel methodology using dicarboxylic acid halides as a spacer for the surface-initiated, covalent immobilization of enzymes onto microporous membranes. One of the reactive carboxyl groups from the dicarboxylic acid halides was immobilized onto the membrane surface and the other was conjugated with an amino group of enzymes via an active ester method. Sebacoyl chloride (SC) and trypsin were used as models of the dicarboxylic acid halide and enzyme, respectively. The effects of the reaction conditions such as reaction temperature, trypsin concentration, reaction time, and SC concentration were investigated on the immobilization efficiency with respect to the surface density, specific activity, and activity retention of the immobilized trypsin. The optimum surface density was 36 μg cm?2, and the corresponding membrane showed an excellent specific activity of 22 U cm?2 with a high activity retention of 26% in a soaking mode. Furthermore, in a filtration mode, these values largely improved to 118 U cm?2 and 145% respectively due to the enhanced diffusion force, meaning that the immobilized trypsin on/in the membrane has higher activity than non-immobilized, native trypsin. In addition, the immobilized trypsin exhibited a remarkable improvement in thermal resistance, continuous operation capability, and reusability. Furthermore, the presented method was also applicable to lipase. This technique provides a practical and simple method to immobilize enzymes and offers a tool to design the membranes used in EMBRs.
机译：在工业过程中，提高酶膜生物反应器（EMBR）中酶的可接受性的主要挑战在于有效地将酶固定在支持物上，同时保持其构象和活性。这项工作描述了一种新颖的方法，该方法使用二羧酸卤化物作为间隔物，用于将酶表面引发的共价固定在微孔膜上。将来自二羧酸卤化物的反应性羧基之一固定在膜表面上，另一个通过活性酯法与酶的氨基缀合。癸二酰氯（SC）和胰蛋白酶分别用作二羧酸卤化物和酶的模型。研究了反应条件如反应温度，胰蛋白酶浓度，反应时间和SC浓度对固定化效率的影响，该效率与固定化胰蛋白酶的表面密度，比活性和活性保留有关。最佳表面密度为36μgcm ？2 ，相应的膜表现出优异的比活度，为22 U cm ？2 在浸泡模式下具有26％的高活性保留。此外，在过滤模式下，由于增强了扩散力，这些值分别大大提高到了118 U cm ？2 和145％，这意味着固定化胰蛋白酶在/上该膜比未固定的天然胰蛋白酶具有更高的活性。另外，固定化的胰蛋白酶在耐热性，连续操作能力和可重复使用性方面显示出显着的改善。此外，提出的方法也适用于脂肪酶。该技术提供了固定酶的实用且简单的方法，并提供了设计用于EMBR的膜的工具。

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