Comparison of initial hydrolysis of the three dimethyl phthalate esters (DMPEs) by a basidiomycetous yeast, Trichosporon DMI-5-1, from coastal sediment
Comparison of initial hydrolysis of the three dimethyl phthalate esters (DMPEs) by a basidiomycetous yeast, Trichosporon DMI-5-1, from coastal sediment
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DOI:
10.1007/s11356-011-0525-1
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发表时间:
2011-05
影响因子:
5.8
通讯作者:
Zhuhua Luo;Yi-Rui Wu;K. Pang;J. Gu;L. Vrijmoed
中科院分区:
文献类型:
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作者:
Zhuhua Luo;Yi-Rui Wu;K. Pang;J. Gu;L. Vrijmoed
PurposeDimethyl phthalate esters (DMPEs) are a group of plasticizers commonly detected in the environment with potential adverse human health impact. The degradation of DMPEs by fungal systems has been studied to a limited extent, particularly by yeasts. In this study, a basidiomycetous yeastTrichosporonDMI-5-1 capable of degrading DMPEs was obtained and the degradation pathways were investigated.ResultsA DMPE-degrading yeast was isolated from costal sediment by enrichment culture technique and was identified asTrichosporonsp. DMI-5-1 based on microscopic morphology and 18S rDNA sequence. Comparative investigations on biodegradation of three isomers of DMPEs, namely dimethyl phthalate (DMP), dimethyl isophthalate (DMI), and dimethyl terephthalate (DMT), were carried out with this yeast strain.Trichosporonsp. DMI-5-1 could not mineralize DMPEs completely but transform them to respective monomethyl phthalate or phthalic acid. Biochemical degradation pathways for the three DMPE isomers byTrichosporonsp. DMI-5-1 were apparently different. The yeast carried out one-step ester hydrolysis of DMP and DMI to respective monoesters (monomethyl phthalate and monomethyl isophthalate, respectively) and no further metabolism of these two monoesters. Meanwhile, DMT was transformed by the yeast to monomethyl terephthalate and subsequently to terephthalic acid by stepwise hydrolysis of the two ester bonds.ConclusionsThis study shows that different catalytic processes are involved in the transformation of DMPEs by the basidiomycetous yeastTrichosporonsp. DMI-5-1 and suggests that its esterases, responsible for the initial hydrolyzing the two ester bonds of DMPEs, are highly substrate specific.