Efficient removal of toxic phthalate by immobilized serine-type aldehyde-tagged esterase G |
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| Institution: | 1. University Children Hospital, Paediatric Haematology, Oncology and Transplantology Department, Lublin, Poland;2. Department of Medical Genetics, University of Cambridge, Cambridge Institute for Medical Research, Cambridge CB2 0XY, UK;3. Department of Physiology, Development and Neuroscience, University of Cambridge, Cambridge CB2 3EG, UK;4. Department of Chemistry, Biochemistry I, Bielefeld University, Bielefeld, Germany;5. University Medical Center Goettingen, Children''s Hospital, Department of Child Neurology, Goettingen, Germany;6. University Children Hospital, Paediatric Haematology, Oncology and Transplantology Department, Cytogenetic Laboratory, Lublin, Poland;7. Institute of Psychiatry and Neurology, Department of Genetics, Warsaw, Poland;1. Division of Cardiology, Department of Medicine, University of California at San Diego, La Jolla, CA;2. Department of Family and Preventive Medicine, University of California at San Diego, San Diego, CA;3. Veterans Affairs San Diego Healthcare System, La Jolla, CA |
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| Abstract: | 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 1 h incubation at 60 °C. Additionally, nearly 100% and over 30% of the DBP in 10 mM and 100 mM solutions, respectively, was degraded by the immobilized EstG within 18 h. |
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| Keywords: | Immobilization Aldehyde tag Phthalate esters Biodegradation Protein modification Sulfatase motif |
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