Cloning of a dibutyl phthalate hydrolase gene from Acinetobacter sp. strain M673 and functional analysis of its expression product in Escherichia coli

Wu, Jun; Liao, Xuewei; Yu, Fang-Bo; Wei, Zhongbo; Yang, Liuyan

doi:10.1007/s00253-012-4232-8

Cited by 80 publications

(41 citation statements)

References 32 publications

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“…Eight esterases with high activity toward pNPB were initially selected and evaluated for their effects on DBP degradation. DBP was used as an indicator because it has an alkyl chain of moderate length, which is suitable for use in determining the PAE's degradation efficiency (16). Among these candidate esterases, a new enzyme cloned from S. acidophilus DSM10332 and designated EstS1 showed very high activities toward both pNPB and DBP, with high thermostability.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Newly Identified Thermostable Esterase from Sulfobacillus acidophilus: Properties and Performance in Phthalate Ester Degradation

Zhang

Fan

Qiu

et al. 2014

Appl Environ Microbiol

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EstS1, a newly identified thermostable esterase from Sulfobacillus acidophilus DSM10332, was heterologously expressed in Escherichia coli and shown to enzymatically degrade phthalate esters (PAEs) to their corresponding monoalkyl PAEs. The optimal pH and temperature of the esterase were found to be 8.0 and 70°C, respectively. The half-life of EstS1 at 60°C was 15 h, indicating that the enzyme had good thermostability. The specificity constant (k cat /K m ) of the enzyme for p-nitrophenyl butyrate was as high as 6,770 mM ؊1 s ؊1 . The potential value of EstS1 was demonstrated by its ability to effectively hydrolyze 35 to 82% of PAEs (10 mM) within 2 min at 37°C, with all substrates being completely degraded within 24 h. At 60°C, the time required for complete hydrolysis of most PAEs was reduced by half. To our knowledge, this enzyme is a new esterase identified from thermophiles that is able to degrade various PAEs at high temperatures.

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Section: Resultsmentioning

confidence: 99%

“…strain YGJ1 (14), dimethyl terephthalate esterase from Fusarium species (15), and dibutyl phthalate (DBP) hydrolase from Acinetobacter sp. strain M673 (16). The last enzyme is the only one in which the corresponding gene and protein have been identified.…”

mentioning

confidence: 99%

Newly Identified Thermostable Esterase from Sulfobacillus acidophilus: Properties and Performance in Phthalate Ester Degradation

Zhang

Fan

Qiu

et al. 2014

Appl Environ Microbiol

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“…Strain Acinetobacter sp. M673 could not grow on PAEs, but the cells could transform these compounds to PA via corresponding monoalkyl phthalates (MAPs) (Wu et al 2013). One DBP hydrolase gene (1095 bp) was identified from a genomic library, which could hydrolyze dialkyl phthalates to the corresponding monoalkyl phthalates.…”

Section: Identification Of Dehp Metabolitesmentioning

confidence: 99%

Biodegradation of phthalic acid esters by a newly isolated Mycobacterium sp. YC-RL4 and the bioprocess with environmental samples

Ren

Yang

Nahurira

et al. 2016

Environ Sci Pollut Res

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Bacterial strain YC-RL4, capable of utilizing phthalic acid esters (PAEs) as the sole carbon source for growth, was isolated from petroleum-contaminated soil. Strain YC-RL4 was identified as Mycobacterium sp. by 16S rRNA gene analysis and Biolog tests. Mycobacterium sp. YC-RL4 could rapidly degrade dibutyl phthalate (DBP), diethyl phthalate (DEP), dimethyl phthalate (DMP), dicyclohexyl phthalate (DCHP), and di-(2-ethylhexyl) phthalate (DEHP) under both individual and mixed conditions, and all the degradation rates were above 85.0 % within 5 days. The effects of environmental factors which might affect the degrading process were optimized as 30 °C and pH 8.0. The DEHP metabolites were detected by HPLC-MS and the degradation pathway was deduced tentatively. DEHP was transformed into phthalic acid (PA) via mono (2-ethylhexyl) phthalate (MEHP) and PA was further utilized for growth via benzoic acid (BA) degradation pathway. Cell surface hydrophobicity (CSH) assays illuminated that the strain YC-RL4 was of higher hydrophobicity while grown on DEHP and CSH increased with the higher DEHP concentration. The degradation rates of DEHP by strain YC-RL4 in different environmental samples was around 62.0 to 83.3 % and strain YC-RL4 survived well in the soil sample. These results suggested that the strain YC-RL4 could be used as a potential and efficient PAE degrader for the bioremediation of contaminated sites.

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“…For some reported esterases, AbMBH has 75 % identity with EstA from Acinetobacter calcoaceticus BD413 [23], 82 % identity with EstA from Acinetobacter lwoffii I6C-1 [24] and EstA from Pseudomonas citronellolis ATCC 13674 [25], and 82 % identity with DPH from Acinetobacter sp. M673 [26]. Among the other characterized esterases, AbMBH shared lower identities (34-37 %) with some thermophilic or hyperthermophilic esterases, including Est from Pyrobaculum calidifontis VA1 (35 % identity) [27], AFEST from Archaeoglobus fulgidus ATCC 49558 (37 %) [28], Sto-Est from Sulfolobus tokodaii DSM 16993 (36 %) [29], Est2 from Alicyclobacillus acidocaldarius (36 %) [30], and EstE1 from a metagenomic library (34 %) [31].…”

Section: Resultsmentioning

confidence: 97%

Cloning and Characterization of an Enantioselective l-Menthyl Benzoate Hydrolase from Acinetobacter sp. ECU2040

Yin

Zheng

et al. 2015

Appl Biochem Biotechnol

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A new esterase gene abmbh, encoding a benzoate hydrolase which can enantioselectively hydrolyze l-menthyl benzoate to l-menthol, was recently identified from the genomic library of a soil isolate Acinetobacter sp. ECU2040. The abmbh gene contains a 1080-bp open reading frame encoding a protein of 360 amino acids with a calculated molecular mass of 40.7 kDa. The corresponding enzyme AbMBH was functionally expressed in Escherichia coli BL21 (DE3), purified, and characterized. The AbMBH displayed the maximum activity towards p-nitrophenyl butyrate at 50 °C, and an optimum pH of 8.5. A K M of 2.6 mM and a k cat of 0.26 s(-1) were observed towards dl-menthyl benzoate. The AbMBH exhibited a moderate enantioselectivity (E = 27.5) towards dl-menthyl benzoate. It can also catalyze the enantioselective hydrolysis of a variety of racemic menthyl esters, including dl-menthyl acetate, dl-menthyl chloroacetate, and dl-menthyl butyrate.

show abstract

Cloning of a dibutyl phthalate hydrolase gene from Acinetobacter sp. strain M673 and functional analysis of its expression product in Escherichia coli

Cited by 80 publications

References 32 publications

Newly Identified Thermostable Esterase from Sulfobacillus acidophilus: Properties and Performance in Phthalate Ester Degradation

Newly Identified Thermostable Esterase from Sulfobacillus acidophilus: Properties and Performance in Phthalate Ester Degradation

Biodegradation of phthalic acid esters by a newly isolated Mycobacterium sp. YC-RL4 and the bioprocess with environmental samples

Cloning and Characterization of an Enantioselective l-Menthyl Benzoate Hydrolase from Acinetobacter sp. ECU2040

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