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首页> 外文期刊>Artificial cells, blood substitutes, and biotechnology >Covalent immobilization of trypsin on glutaraldehyde-activated silica for protein fragmentation.
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Covalent immobilization of trypsin on glutaraldehyde-activated silica for protein fragmentation.

机译：将胰蛋白酶共价固定在戊二醛活化的二氧化硅上以进行蛋白质裂解。

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摘要

Trypsin was immobilized by covalent binding to glutaraldehyde-activated silica with and without a spacer arm; 1,6-diaminohexane and polyethyleneglycol as well. The addition of polyethyleneglycol (PEG) to the immobilization media increased the activity of immobilized trypsin in organic solvents, whilst free trypsin activity disappeared under the same conditions. Thermal, pH, storage, and operational stabilities of the free and immobilized enzyme were found to be better than the free enzyme. Furthermore, use of immobilized enzyme for protein fragmentation was achieved by solid-phase, on-line, protein digestion in organic solvents. Reaction times were reduced to a few minutes and the sample handling was minimized.
机译：通过与或不与间隔臂共价结合，将胰蛋白酶固定在戊二醛活化的二氧化硅上。 1,6-二氨基己烷和聚乙二醇也是如此。将聚乙二醇（PEG）添加到固定化介质中可提高固定化胰蛋白酶在有机溶剂中的活性，而游离胰蛋白酶活性在相同条件下消失。发现游离和固定化酶的热，pH，储存和操作稳定性优于游离酶。此外，通过在有机溶剂中进行固相在线蛋白质消化可以实现固定化酶用于蛋白质片段化。反应时间减少至几分钟，并且样品处理量降至最低。

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