File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Transformation of dimethyl phthalate, dimethyl isophthalate and dimethyl terephthalate by Rhodococcus rubber Sa and modeling the processes using the modified Gompertz model

TitleTransformation of dimethyl phthalate, dimethyl isophthalate and dimethyl terephthalate by Rhodococcus rubber Sa and modeling the processes using the modified Gompertz model
Authors
KeywordsBiotransformation
Dimethyl isophthalate
Dimethyl phthalate
Dimethyl terephthalate
Gompertz model
Mixed substrates
Issue Date2005
PublisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/ibiod
Citation
International Biodeterioration And Biodegradation, 2005, v. 55 n. 3, p. 223-232 How to Cite?
AbstractPhthalate ester isomers, including dimethyl phthalate (DMP), dimethyl isophthalate (DMI) and dimethyl terephthalate (DMT), were found to be transformed by Rhodococcus rubber Sa isolated from a mangrove sediment using DMT as a carbon source initially. At a concentration of 80 mg l -1, transformation of DMP, DMI and DMT was achieved in 9, 1 and 5 days, respectively. During the hydrolytical transformation of DMP, DMI and DMT, their corresponding intermediates were identified as mono-methyl phthalate (MMP), mono-methyl isophthalate (MMI) and mono-methyl terephthalate (MMT), suggesting that transformation of all three isomers followed an identical biochemical pathway of de-esterification. However, none of the produced monoesters was further transformed by R. rubber Sa and they accumulated in the culture media during incubation. It seems that further transformation of monoesters require a set of hydrolytic enzymes different from those involved in the first transformation reaction. Kinetics of DMT, DMI and DMP transformation was well described by the modified Gompertz model independent of the individual substrate condition or a mixture of the three isomers. Both DMI and DMT were easier transformed substrates than DMP, resulting in higher maximum transformation rate (R m) and shorter lag time phase (λ) derived from the modified Gompertz model. The modified Gompertz model based on one-substrate system can be used in fitting transformation kinetics of mixture substrate system. Our data suggest that degradation of phthalate diesters involves different enzymes in the hydrolysis of the two identical ester groups. © 2005 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/73321
ISSN
2023 Impact Factor: 4.1
2023 SCImago Journal Rankings: 0.990
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLi, Jen_HK
dc.contributor.authorGu, JDen_HK
dc.contributor.authorPan, Len_HK
dc.date.accessioned2010-09-06T06:50:12Z-
dc.date.available2010-09-06T06:50:12Z-
dc.date.issued2005en_HK
dc.identifier.citationInternational Biodeterioration And Biodegradation, 2005, v. 55 n. 3, p. 223-232en_HK
dc.identifier.issn0964-8305en_HK
dc.identifier.urihttp://hdl.handle.net/10722/73321-
dc.description.abstractPhthalate ester isomers, including dimethyl phthalate (DMP), dimethyl isophthalate (DMI) and dimethyl terephthalate (DMT), were found to be transformed by Rhodococcus rubber Sa isolated from a mangrove sediment using DMT as a carbon source initially. At a concentration of 80 mg l -1, transformation of DMP, DMI and DMT was achieved in 9, 1 and 5 days, respectively. During the hydrolytical transformation of DMP, DMI and DMT, their corresponding intermediates were identified as mono-methyl phthalate (MMP), mono-methyl isophthalate (MMI) and mono-methyl terephthalate (MMT), suggesting that transformation of all three isomers followed an identical biochemical pathway of de-esterification. However, none of the produced monoesters was further transformed by R. rubber Sa and they accumulated in the culture media during incubation. It seems that further transformation of monoesters require a set of hydrolytic enzymes different from those involved in the first transformation reaction. Kinetics of DMT, DMI and DMP transformation was well described by the modified Gompertz model independent of the individual substrate condition or a mixture of the three isomers. Both DMI and DMT were easier transformed substrates than DMP, resulting in higher maximum transformation rate (R m) and shorter lag time phase (λ) derived from the modified Gompertz model. The modified Gompertz model based on one-substrate system can be used in fitting transformation kinetics of mixture substrate system. Our data suggest that degradation of phthalate diesters involves different enzymes in the hydrolysis of the two identical ester groups. © 2005 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/ibioden_HK
dc.relation.ispartofInternational Biodeterioration and Biodegradationen_HK
dc.subjectBiotransformationen_HK
dc.subjectDimethyl isophthalateen_HK
dc.subjectDimethyl phthalateen_HK
dc.subjectDimethyl terephthalateen_HK
dc.subjectGompertz modelen_HK
dc.subjectMixed substratesen_HK
dc.titleTransformation of dimethyl phthalate, dimethyl isophthalate and dimethyl terephthalate by Rhodococcus rubber Sa and modeling the processes using the modified Gompertz modelen_HK
dc.typeArticleen_HK
dc.identifier.emailGu, JD: jdgu@hkucc.hku.hken_HK
dc.identifier.authorityGu, JD=rp00701en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.ibiod.2004.12.003en_HK
dc.identifier.scopuseid_2-s2.0-15944368633en_HK
dc.identifier.hkuros98029en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-15944368633&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume55en_HK
dc.identifier.issue3en_HK
dc.identifier.spage223en_HK
dc.identifier.epage232en_HK
dc.identifier.isiWOS:000228414000008-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLi, J=8951695400en_HK
dc.identifier.scopusauthoridGu, JD=7403129601en_HK
dc.identifier.scopusauthoridPan, L=54393873900en_HK
dc.identifier.issnl0964-8305-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats