4 years ago

Efficient removal of toxic phthalate by immobilized serine-type aldehyde-tagged esterase G

Efficient removal of toxic phthalate by immobilized serine-type aldehyde-tagged esterase G
Esterase G (EstG) from dibutyl phthalate (DBP)-degrading Sphingobium sp. SM42 was immobilized on amine-functionalized supports through aldehyde tag technology. Two different sulfatase motif tags, either LCTPSR (cysteine-type) or MSAPAR (serine-type), each of which is recognized by a specific formylglycine generating enzyme (FGE), were fused to the C-terminus of EstG. The cysteine-specific FGE was derived from Pseudomonas putida KT2440 while Klebsiella sp. SLS5 provided serine-specific FGE. The EstG with serine-type aldehyde tag showed a greater immobilization yield and higher specific activity by 4.8-fold and 1.8-fold, respectively. The immobilized EstG retained over 90% of its original activity after seven cycles of usage, and exhibited significantly improved thermostability by retaining 66% activity after 1h incubation at 60°C. Additionally, nearly 100% and over 30% of the DBP in 10mM and 100mM solutions, respectively, was degraded by the immobilized EstG within 18h.

Publisher URL: www.sciencedirect.com/science

DOI: S1359511317301095

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