Degradation of an endocrine disrupting chemical, DEHP [di-(2-ethylhexyl)- phthalate], by Fusarium oxysporum f. sp. pisi cutinase

Y. H. Kim, J. Lee, S. H. Moon

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59 Citations (Scopus)


The efficiency of two lypolytic enzymes (fungal cutinase, yeast esterase) in the degradation of di-(2-ethylhexyl)-phthalate (DEHP) was investigated. The DEHP-degradation rate of fungal cutinase was surprisingly high, i.e. almost 70% of the initial DEHP (500 mg/l) was decomposed within 2.5 h and nearly 50% of the degraded DEHP disappeared within the initial 15 min. With the yeast esterase, despite the same concentration, more than 85% of the DEHP remained even after 3 days of treatment. During the enzymatic degradation of DEHP, several DEHP-derived compounds were detected and time-course changes in composition were also monitored. During degradation with fungal cutinase, most DEHP was converted into 1,3-isobenzofurandione (IBF) by diester hydrolysis. In the degradation by yeast esterase, two organic chemicals were produced from DEHP: IBF and an unidentified compound (X). The final chemical composition after 3 days was significantly dependent on the enzyme used. Fungal cutinase produced IBF as a major degradation compound. However, in the DEHP degradation by yeast esterase, compound X was produced in abundance in addition to IBF. The toxic effects of the final degradation products were investigated, using various recombinant bioluminescent bacteria and, as a result, the degradation products from yeast esterase were shown to contain a toxic hazard, causing oxidative stress and damage to protein synthesis.

Original languageEnglish
Pages (from-to)75-80
Number of pages6
JournalApplied Microbiology and Biotechnology
Issue number1
Publication statusPublished - 2003 Nov

Bibliographical note

Copyright 2008 Elsevier B.V., All rights reserved.

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology


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