The catalytically-active inclusion bodies (CatIBs) represent a promising strategy for immobilizing enzyme without additional carriers and chemicals, which has aroused great attention in academic and industrial communities. In this work, we discovered two natural parallel right-handed coiled-coil tetramer peptides from PDB database by a structural mining strategy. The two self-assembling peptides, NSPdoT from rotavirus and HVdoT from human Vasodilator-stimulated phosphoprotein, efficiently induced the CatIBs formation of a (R)-Hydroxynitrile lyase from Arabidopsis thaliana (AtHNL) in Escherichia coli cells. This is convenient to simultaneously purify and immobilize the target proteins as biocatalysts. As expected, HVdoT-AtHNL and NSPdoT-AtHNL possessed drastically increased tolerance toward lower pH values, which will be very critical to synthesize cyanohydrins under acidic condition for suppressing the non-enzymatic side reaction. In addition. AtHNL-CatIBs are produced at high yield in host cells as bioactive microparticles, which exhibited high thermal and pH stabilities. Therefore, the CatIBs method represent a promising application for the immobilization of enzymes in the biocatalysis field.

催化活性包涵体（CatIBs）代表了一种无需额外载体和化学品即可固定酶的有前景的策略，这引起了学术界和工业界的极大关注。在这项工作中，我们通过结构挖掘策略从 PDB 数据库中发现了两种天然平行的右手卷曲螺旋四聚体肽。两种自组装肽，来自轮状病毒的 NSPdoT 和来自人血管扩张剂刺激的磷蛋白的 HVdoT，在大肠杆菌细胞中有效诱导来自拟南芥( At HNL)的 ( R )-羟基腈裂解酶的 CatIBs 形成。这便于同时纯化和固定目标蛋白质作为生物催化剂。正如预期的那样，HVdoT-At HNL 和 NSPdoT- At HNL 对较低的 pH 值具有显着增加的耐受性，这对于在酸性条件下合成氰醇以抑制非酶促副反应非常关键。此外。在HNL-CatIBs 在宿主细胞中作为生物活性微粒以高产率产生，其表现出高的热稳定性和 pH 稳定性。因此，CatIBs 方法代表了生物催化领域酶固定化的一个有前景的应用。