Purification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalate

Luo, Zengwei; Wu, Yi-Rui; Chow, Raymond K.K.; Luo, Jingjing; Gu, Ji‐Dong; Vrijmoed, L. L. P.

doi:10.1016/j.procbio.2012.01.015

Cited by 47 publications

(19 citation statements)

References 32 publications

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“…Above 55°C, EreB lost its activity but erythromycin was auto-degraded by heat (about 30% thermal auto-degradation). This phenomenon had already been observed in previous studies [38]. Therefore, working at high temperatures is unnecessary as this might hinder biocatalyst activity, making the enzymatic process useless.…”

Section: Effects Of Ph and Temperaturesupporting

confidence: 56%

Erythromycin degradation by esterase (EreB) in enzymatic membrane reactors

Cazes

Belleville

Petit

et al. 2016

Biochemical Engineering Journal

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Section: Effects Of Ph and Temperaturesupporting

confidence: 56%

Erythromycin degradation by esterase (EreB) in enzymatic membrane reactors

Cazes

Belleville

Petit

et al. 2016

Biochemical Engineering Journal

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“…They are also supplied as additives in paints, adhesives, cardboard, lubricants, and fragrances (Luo et al 2012). The common structure of PAEs is composed of a benzene ring and two side chains at the orthoposition.…”

mentioning

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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“…Only a few enzymes involved in this reaction have been reported, such as PAE hydrolase from Micrococcus sp. strain YGJ1 (14), dimethyl terephthalate esterase from Fusarium species (15), and dibutyl phthalate (DBP) hydrolase from Acinetobacter sp. strain M673 (16).…”

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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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.

show abstract

Purification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalate

Cited by 47 publications

References 32 publications

Erythromycin degradation by esterase (EreB) in enzymatic membrane reactors

Erythromycin degradation by esterase (EreB) in enzymatic membrane reactors

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

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

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