Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy.
Department of Chemistry and Technology of Drugs, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy.
Int J Mol Sci. 2022 Jun 10;23(12):6529. doi: 10.3390/ijms23126529.
Amine oxidases are enzymes belonging to the class of oxidoreductases that are widespread, from bacteria to humans. The amine oxidase from has recently appeared in the landscape of biocatalysis, showing good potential in the green synthesis of aldehydes. This enzyme catalyzes the oxidative deamination of a wide range of primary amines into the corresponding aldehydes but its use as a biocatalyst is challenging due to the possible inactivation that might occur at high product concentrations. Here, we show that the enzyme's performance can be greatly improved by immobilization on solid supports. The best results are achieved using amino-functionalized magnetic microparticles: the immobilized enzyme retains its activity, greatly improves its thermostability (4 h at 75 °C), and can be recycled up to 8 times with a set of aromatic ethylamines. After the last reaction cycle, the overall conversion is about 90% for all tested substrates, with an aldehyde production ranging between 100 and 270 mg depending on the substrate used. As a proof concept, one of the aldehydes thus produced was successfully used for the biomimetic synthesis of a non-natural benzylisoquinoline alkaloid.
胺氧化酶属于氧化还原酶类,广泛存在于从细菌到人类的生物体中。 最近, 来源的胺氧化酶出现在生物催化领域,在醛的绿色合成中显示出良好的潜力。 该酶催化广泛的伯胺的氧化脱氨作用,生成相应的醛,但由于在高产物浓度下可能发生的失活,其作为生物催化剂的使用具有挑战性。 在这里,我们表明通过固定在固体载体上可以大大提高酶的性能。 使用氨基功能化的磁性微球获得最佳结果:固定化酶保留其活性,大大提高其热稳定性(75°C 下 4 小时),并可在一组芳香族乙胺中回收 8 次以上。 在最后一次反应循环后,对于所有测试的底物,总体转化率约为 90%,根据所用的底物,醛的产量在 100 至 270mg 之间。 作为概念验证,由此产生的一种醛成功地用于非天然苄基异喹啉生物碱的仿生合成。