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脂相间-纳米受限水中苯甲醛裂解酶的低温活性和稳定性。

Cryogenic activity and stability of benzaldehyde lyase enzyme in lipidic mesophases-nanoconfined water.

机构信息

Department of Health Sciences and Technology, ETH Zürich, 8092 Zurich, Switzerland.

出版信息

Chem Commun (Camb). 2021 Jun 8;57(46):5650-5653. doi: 10.1039/d1cc01315g.

Abstract

Phytantriol-based lipidic mesophases (LMs) are introduced as a platform for cryoenzymology, which relies on the presence of liquid water in LMs at subzero temperatures. After incorporation into LMs, the model enzyme Benzaldehyde lyase (BAL) shows high cryogenic stability and activity. In contrast, BAL in bulk solution undergoes significant secondary structural transitions caused by low temperatures (cold denaturation), demonstrating the potential of this approach to enable in meso cryoenzymology.

摘要

基于植物三醇的类脂相(LMs)被引入作为低温酶学的平台,该方法依赖于在亚零温度下 LMs 中液态水的存在。在掺入 LMs 后,模型酶苯甲醛裂解酶(BAL)表现出高的低温稳定性和活性。相比之下,在本体溶液中的 BAL 会因低温而发生显著的二级结构转变(冷变性),这表明该方法有可能实现中温低温酶学。

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