The Effect of Visible Light on the Catalytic Activity of PLP-Dependent Enzymes.
The Effect of Visible Light on the Catalytic Activity of PLP-Dependent Enzymes.
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DOI：
10.1002/cctc.202100163
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发表时间：
2021-05-19
期刊：
影响因子：
4.5
通讯作者：
Rother D
中科院分区：
文献类型：
--
作者：
Gerlach T;Nugroho DL;Rother D
依赖于吡哆醛5‘-磷酸(PLP)的酶是一类用途广泛的生物催化剂，具有多种工业应用。然而，PLP是光敏性的，在某些光条件下会导致酶失活。由于大多数依赖PLP的酶通常不在黑暗条件下处理，我们评估了可见光对生产和转化过程中依赖PLP的酶活性的影响。我们检测了来自紫罗兰色杆菌、巨大芽孢杆菌、河弧菌和节杆菌变种的四种氨基转氨酶，以及来自瘤胃单胞菌的两种赖氨酸脱羧酶和来自大肠杆菌的低密度脂蛋白。似乎这六种酶中有五种在实验室光照条件下处理时活性显著下降，最高可达90 %。令人惊讶的是，只有节杆菌的氨基转移酶变异体似乎不受光照的影响，甚至在6 h的过程中显示出对150 %的相对活性，而无论光照条件如何。注意光线：在这项工作中，研究表明，依赖PLP的酶的活性可以受到光照的影响，即使是普通的实验室或阳光。大多数被测试的酶都表现出明显的活性丧失。因此，通过在黑暗中进行酶的产生和反应，可以极大地提高催化活性。然而，一种依赖PLP的酶似乎完全抵抗任何类型的光照。
Pyridoxal 5’‐phosphate (PLP)‐dependent enzymes are a versatile class of biocatalysts and feature a variety of industrial applications. However, PLP is light sensitive and can cause inactivation of enzymes in certain light conditions. As most of the PLP‐dependent enzymes are usually not handled in dark conditions, we evaluated the effect of visible light on the activity of PLP‐dependent enzymes during production as well as transformation. We tested four amine transaminases, from Chromobacterium violaceum, Bacillus megaterium, Vibrio fluvialis and a variant from Arthrobacter species as well as two lysine decarboxylases, from Selenomonas ruminantium and the LDCc from Escherichia coli. It appeared that five of these six enzymes suffered from a significant decrease in activity by up to 90 % when handled in laboratory light conditions. Surprisingly, only the amine transaminase variant from Arthrobacter species appeared to be unaffected by light exposure and even showed an activation to 150 % relative activity over the course of 6 h regardless of the light conditions. Careful with light: In this work, it is shown that the activity of PLP‐dependent enzymes can be affected by illumination, even by ordinary laboratory or sunlight. Most of the enzymes tested showed a significant loss of activity. Consequently, by performing enzyme production and reaction in the dark, the catalytic activity could be increased immensely. However, one PLP‐dependent enzyme appeared to be completely resistant to any type of illumination.
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