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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Variant of the Thermomyces lanuginosus lipase with improved kinetic stability: A candidate for enzyme replacement therapy
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Variant of the Thermomyces lanuginosus lipase with improved kinetic stability: A candidate for enzyme replacement therapy

机译：具有改善的动力学稳定性的嗜热单胞菌脂肪酶的变体：酶替代疗法的候选者

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摘要

Lipases with high kinetic stability and enzymatic efficiency in the human gastro-intestinal tract may help against exocrine pancreatic insufficiency. Here we mimic gastric conditions to study how bile salts and pH affect the stability and activity of Thermomyces lanuginosus lipase (TIL) and its stabler variant StL using spec-troscopy, calorimetry and gel electrophoresis. Both enzymes resist trypsin digestion with and without bile salts. Bile salts activate native TIL and StL equally well, bind weakly to denatured TIL and StL at lower pH and precipitate native TIL and StL at pH 4. StL refolds more efficiently than TIL from gastric pH in bile salts, regaining activity when refolding from pH as low as 1.8 and above while TIL cannot go below pH 2.6. StL also unfolds 10-40 fold more slowly in the denaturant guanidinium chloride and the anionic surfactant SDS. We ascribe StL's superior performance to general alterations in its electrostatic potential which makes it more acid-resistant. These superior properties make StL a good candidate for pancreatic enzyme replacement therapy.
机译：在人胃肠道中具有高动力学稳定性和酶促效率的脂肪酶可能​​有助于抵抗外分泌性胰腺功能不全。在这里，我们通过光谱法，量热法和凝胶电泳，模拟胃部条件，研究胆汁盐和pH值如何影响嗜热单胞菌脂肪酶（TIL）及其更稳定的变体StL的稳定性和活性。两种酶都可以抵抗有或没有胆汁盐的胰蛋白酶消化。胆汁盐同样能很好地激活天然TIL和StL，在较低的pH下与变性TIL和StL弱结合，并在pH 4下沉淀天然TIL和StL。在胃液中，胆汁盐中的StL比TIL更有效地重折叠，当从pH重新折叠时，其恢复活性低至1.8及以上，而TIL不能低于pH 2.6。 StL在变性氯化胍和阴离子表面活性剂SDS中的展开速度也要慢10-40倍。我们将StL的卓越性能归因于其静电势的一般改变，从而使其更具耐酸性。这些优异的特性使StL成为胰腺酶替代疗法的良好候选者。

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