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The Effect of Visible Light on the Catalytic Activity of PLP‐Dependent Enzymes
Author(s) -
Gerlach Tim,
Nugroho David Limanhadi,
Rother Dörte
Publication year - 2021
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.202100163
Subject(s) - enzyme , biochemistry , chemistry , transaminase , pyridoxal , arthrobacter , pyridoxal phosphate , chromobacterium violaceum , bacillus sphaericus , biology , bacteria , cofactor , bacillales , bacillus subtilis , gene , quorum sensing , virulence , genetics
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.