Biodegradation of dipropyl phthalate and toxicity of its degradation products

A comparison of Fusarium oxysporum f. sp. pisi cutinase and Candida cylindracea esterase

Yang Hoon Kim, Jiho Min, Kyung Dong Bae, Man Bock Gu, Jeewon Lee

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The efficiency of two lypolytic enzymes (fungal cutinase, yeast esterase) in the degradation of dipropyl phthalate (DPrP) was investigated. The DPrP-degradation rate of fungal cutinase was surprisingly high, i.e., almost 70% of the initial DPrP (500 mg/l) was decomposed within 2.5 h and nearly 50% of the degraded DPrP disappeared within the initial 15 min. With the yeast esterase, despite the same concentration, more than 90% of the DPrP remained even after 3 days of treatment. During the enzymatic degradation of DPrP, several DPrP-derived compounds were detected and time-course changes in composition were also monitored. The final chemical composition after 3 days was significantly dependent on the enzyme used. During degradation with fungal cutinase, most DPrP was converted into 1,3-isobenzofurandione (IBF) by diester hydrolysis. However, in the degradation by yeast esterase, propyl methyl phthalate (PrMP) was produced in abundance in addition to IBF. The toxic effects of the final degradation products were investigated using various recombinant bioluminescent bacteria. As a result, the degradation products (including PrMP) from yeast esterase severely caused oxidative stress and damage to protein synthesis in bacterial cells, while in the fungal cutinase processes, DPrP was significantly degraded to non-toxic IBF after the extended period (3 days).

Original languageEnglish
Pages (from-to)25-31
Number of pages7
JournalArchives of Microbiology
Volume184
Issue number1
DOIs
Publication statusPublished - 2005 Oct 1

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Candida
Fusarium
Esterases
Biodegradation
Toxicity
Degradation
Yeast
Yeasts
phthalic acid
cutinase
Oxidative stress
Poisons
Enzymes
Chemical analysis
Hydrolysis
Bacteria
Oxidative Stress

Keywords

  • Biodegradation of dipropyl phthalate
  • Cutinase
  • Esterase
  • Recombinant bioluminescent bacteria
  • Toxicity monitoring

ASJC Scopus subject areas

  • Microbiology

Cite this

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title = "Biodegradation of dipropyl phthalate and toxicity of its degradation products: A comparison of Fusarium oxysporum f. sp. pisi cutinase and Candida cylindracea esterase",
abstract = "The efficiency of two lypolytic enzymes (fungal cutinase, yeast esterase) in the degradation of dipropyl phthalate (DPrP) was investigated. The DPrP-degradation rate of fungal cutinase was surprisingly high, i.e., almost 70{\%} of the initial DPrP (500 mg/l) was decomposed within 2.5 h and nearly 50{\%} of the degraded DPrP disappeared within the initial 15 min. With the yeast esterase, despite the same concentration, more than 90{\%} of the DPrP remained even after 3 days of treatment. During the enzymatic degradation of DPrP, several DPrP-derived compounds were detected and time-course changes in composition were also monitored. The final chemical composition after 3 days was significantly dependent on the enzyme used. During degradation with fungal cutinase, most DPrP was converted into 1,3-isobenzofurandione (IBF) by diester hydrolysis. However, in the degradation by yeast esterase, propyl methyl phthalate (PrMP) was produced in abundance in addition to IBF. The toxic effects of the final degradation products were investigated using various recombinant bioluminescent bacteria. As a result, the degradation products (including PrMP) from yeast esterase severely caused oxidative stress and damage to protein synthesis in bacterial cells, while in the fungal cutinase processes, DPrP was significantly degraded to non-toxic IBF after the extended period (3 days).",
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T2 - A comparison of Fusarium oxysporum f. sp. pisi cutinase and Candida cylindracea esterase

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AU - Min, Jiho

AU - Bae, Kyung Dong

AU - Gu, Man Bock

AU - Lee, Jeewon

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AB - The efficiency of two lypolytic enzymes (fungal cutinase, yeast esterase) in the degradation of dipropyl phthalate (DPrP) was investigated. The DPrP-degradation rate of fungal cutinase was surprisingly high, i.e., almost 70% of the initial DPrP (500 mg/l) was decomposed within 2.5 h and nearly 50% of the degraded DPrP disappeared within the initial 15 min. With the yeast esterase, despite the same concentration, more than 90% of the DPrP remained even after 3 days of treatment. During the enzymatic degradation of DPrP, several DPrP-derived compounds were detected and time-course changes in composition were also monitored. The final chemical composition after 3 days was significantly dependent on the enzyme used. During degradation with fungal cutinase, most DPrP was converted into 1,3-isobenzofurandione (IBF) by diester hydrolysis. However, in the degradation by yeast esterase, propyl methyl phthalate (PrMP) was produced in abundance in addition to IBF. The toxic effects of the final degradation products were investigated using various recombinant bioluminescent bacteria. As a result, the degradation products (including PrMP) from yeast esterase severely caused oxidative stress and damage to protein synthesis in bacterial cells, while in the fungal cutinase processes, DPrP was significantly degraded to non-toxic IBF after the extended period (3 days).

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