Journal Article FZJ-2021-01267

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The Effect of Visible Light on the Catalytic Activity of PLP‐Dependent Enzymes

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2021
WILEY-VCH Verlag Weinheim

ChemCatChem 13(10), 2398-2406 () [10.1002/cctc.202100163]

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Abstract: 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.

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Note: This project was funded by the European Research Council in frame of ERC starting grant 757320 „Light Controlled Synthetic Enzyme Cascades”.

Contributing Institute(s):
  1. Biotechnologie (IBG-1)
Research Program(s):
  1. 2171 - Biological and environmental resources for sustainable use (POF4-217) (POF4-217)

Appears in the scientific report 2021
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Medline ; Creative Commons Attribution-NonCommercial CC BY-NC 4.0 ; OpenAccess ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; DEAL Wiley ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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 Datensatz erzeugt am 2021-03-03, letzte Änderung am 2022-09-30