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HERO ID
2854987
Reference Type
Journal Article
Title
Properties of a newly identified esterase from Bacillus sp. K91 and its novel function in diisobutyl phthalate degradation
Author(s)
Ding, J; Wang, C; Xie, Z; Li, J; Yang, Y; Mu, Y; Tang, X; Xu, B; Zhou, J; Huang, Z
Year
2015
Is Peer Reviewed?
1
Journal
PLoS ONE
EISSN:
1932-6203
Publisher
Public Library of Science
Location
San Francisco
Volume
10
Issue
3
Page Numbers
e0119216
Language
English
PMID
25746227
DOI
10.1371/journal.pone.0119216
Web of Science Id
WOS:000350689400057
URL
https://www.proquest.com/scholarly-journals/properties-newly-identified-esterase-bacillus-sp/docview/1661102288/se-2
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Abstract
The widely used plasticizer phthalate esters (PAEs) have become a public concern because of their effects on environmental contamination and toxicity on mammals. However, the biodegradation of PAEs, especially diisobutyl phthalate (DiBP), remains poorly understood. In particular, genes involved in the hydrolysis of these compounds were not conclusively identified. In this study, the CarEW gene, which encodes an enzyme that is capable of hydrolyzing ρ-nitrophenyl esters of fatty acids, was cloned from a thermophilic bacterium Bacillus sp. K91 and heterologously expressed in Escherichia coli BL21 using the pEASY-E2 expression system. The enzyme showed a monomeric structure with a molecular mass of approximately 53.76 kDa and pI of 4.88. The enzyme exhibited maximal activity at pH 7.5 and 45 °C, with ρ-NP butyrate as the best substrate. The enzyme was fairly stable within the pH range from 7.0 to 8.5. High-pressure liquid chromatography (HPLC) and electrospray ionization mass spectrometry (ESI-MS) were employed to detect the catabolic pathway of DiBP. Two intermediate products were identified, and a potential biodegradation pathway was proposed. Altogether, our findings present a novel DiBP degradation enzyme and indicate that the purified enzyme may be a promising candidate for DiBP detoxification and for environmental protection.
Keywords
Sciences: Comprehensive Works; Esterases; Phthalates; Sequence motif analysis; Hydrolases; Sequence alignment; Enzymes; Sequence databases; Laboratories; Mass spectrometry; Toxicity; Biodegradation; Contamination; Ionization; Biomass energy; Proteins; Environmental protection; Fatty acids; pH effects; Mass spectroscopy; Engineering research; Education; Detoxification; Volatile organic compounds--VOCs; Environmental effects; Molecular structure; Public concern; Esterase; Phthalate esters; Substrates; Cloning; Sustainable development; High performance liquid chromatography; Liquid chromatography; High-performance liquid chromatography; Microorganisms; Chromatography; Fusarium oxysporum; Gordonia; Escherichia coli; Bacillus; Acinetobacter; Micrococcus
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IRIS
•
Diisobutyl Phthalate (DIBP) Final
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