We report here a novel observation that immobilization of heparinase I on CNBr-activated Sepharose results in heparin degradation properties that are different from heparinase I in the free solution form. Studies over a range of pHs (5–8) and temperatures (5–50°C) as well as under batch and flow conditions show that immobilized heparinase 1 displays altered pH and temperature optima, and a higher propensity for generation of longer chains (hexa- and octa-) with variable sulfation as compared to that in the free form, which is known to yield disaccharides. The immobilized enzyme retained good eliminase activity over at least five cycles of reuse. In combination, results suggest that heparinase I immobilization may offer a more productive route to longer, variably sulfated sequences.

中文翻译：

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固定化改变了肝素的酶切性质

我们在这里报告了一个新颖的观察结果，即肝素酶I在CNBr活化的琼脂糖凝胶上的固定导致肝素降解特性与游离溶液形式的肝素酶I不同。在一系列pH（5-8）和温度（5-50°C）以及批次和流动条件下的研究表明，固定化肝素酶1的pH和温度最佳值发生了变化，并且产生更长链的倾向更高（与游离形式的硫酸盐相比，硫酸盐具有可变的硫酸盐化作用，后者可产生二糖。固定化酶在至少五个重复使用循环中保持了良好的消除酶活性。结合起来，结果表明肝素酶I的固定化可能为更长的，可变硫酸盐化的序列提供一条更高产的途径。