Manganese peroxidase h4 isozyme mediated degradation and detoxification of triarylmethane dye malachite green: optimization of decolorization by response surface methodology.
Identifieur interne : 000368 ( Main/Exploration ); précédent : 000367; suivant : 000369Manganese peroxidase h4 isozyme mediated degradation and detoxification of triarylmethane dye malachite green: optimization of decolorization by response surface methodology.
Auteurs : Thiyagarajan Saravanakumar [Corée du Sud] ; Thayumanavan Palvannan ; Dae-Hyuk Kim ; Seung-Moon ParkSource :
- Applied biochemistry and biotechnology [ 1559-0291 ] ; 2013.
Descripteurs français
- KwdFr :
- Agents colorants (analyse), Agents colorants (composition chimique), Agents colorants (toxicité), Dépollution biologique de l'environnement (MeSH), Magenta I (analyse), Magenta I (métabolisme), Magenta I (toxicité), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (isolement et purification), Peroxidases (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (isolement et purification), Protéines fongiques (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (isolement et purification), Protéines recombinantes (métabolisme).
- MESH :
- analyse : Agents colorants, Magenta I.
- composition chimique : Agents colorants, Peroxidases, Protéines fongiques, Protéines recombinantes.
- enzymologie : Phanerochaete.
- génétique : Peroxidases, Phanerochaete, Protéines fongiques, Protéines recombinantes.
- isolement et purification : Peroxidases, Protéines fongiques, Protéines recombinantes.
- métabolisme : Magenta I, Peroxidases, Protéines fongiques, Protéines recombinantes.
- toxicité : Agents colorants, Magenta I.
- Dépollution biologique de l'environnement.
English descriptors
- KwdEn :
- Biodegradation, Environmental (MeSH), Coloring Agents (analysis), Coloring Agents (chemistry), Coloring Agents (toxicity), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (isolation & purification), Fungal Proteins (metabolism), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (isolation & purification), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Rosaniline Dyes (analysis), Rosaniline Dyes (metabolism), Rosaniline Dyes (toxicity).
- MESH :
- chemical , analysis : Coloring Agents, Rosaniline Dyes.
- chemical , chemistry : Coloring Agents, Fungal Proteins, Peroxidases, Recombinant Proteins.
- chemical , genetics : Fungal Proteins, Peroxidases, Recombinant Proteins.
- chemical , isolation & purification : Fungal Proteins, Peroxidases, Recombinant Proteins.
- chemical , metabolism : Fungal Proteins, Peroxidases, Recombinant Proteins, Rosaniline Dyes.
- chemical , toxicity : Coloring Agents, Rosaniline Dyes.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- Biodegradation, Environmental.
Abstract
A cDNA encoding for manganese peroxidase isozyme H4 (MnPH4), isolated from Phanerochaete chrysosporium, was expressed in Pichia pastoris, under the control of alcohol oxidase I promoter. The recombinant MnPH4 was efficiently secreted onto media supplemented with hemin at a maximum concentration of 500 U/L, after which purified rMnPH4 was used to decolorize the triarylmethane dye malachite green (MG). Response surface methodology (RSM) was employed to optimize three different operational parameters for the decolorization of MG. RSM showed that the optimized variables of enzyme (0.662 U), MnSO4 (448 μM), and hydrogen peroxide (159 μM) decolorized 100 mg/L of MG completely at 3 h. Additionally, UV-VIS spectra, high-performance liquid chromatography, gas chromatography-mass spectrometry, and liquid chromatography-electrospray ionization/mass spectrometry analysis confirmed the degradation of MG by the formation of main metabolites 4-dimethylamino-benzophenone hydrate, N, N-dimethylaniline (N,N-dimethyl-benzenamine), and methylbenzaldehyde. Interestingly, it was found that rMnPH4 mediates hydroxyl radical attack on the central carbon of MG. Finally, rMnPH4 degraded MG resulted in the complete removal of its toxicity, which was checked under in vitro conditions.
DOI: 10.1007/s12010-013-0220-4
PubMed: 23604969
Affiliations:
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Environmental</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dépollution biologique de l'environnement</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A cDNA encoding for manganese peroxidase isozyme H4 (MnPH4), isolated from Phanerochaete chrysosporium, was expressed in Pichia pastoris, under the control of alcohol oxidase I promoter. The recombinant MnPH4 was efficiently secreted onto media supplemented with hemin at a maximum concentration of 500 U/L, after which purified rMnPH4 was used to decolorize the triarylmethane dye malachite green (MG). Response surface methodology (RSM) was employed to optimize three different operational parameters for the decolorization of MG. RSM showed that the optimized variables of enzyme (0.662 U), MnSO4 (448 μM), and hydrogen peroxide (159 μM) decolorized 100 mg/L of MG completely at 3 h. Additionally, UV-VIS spectra, high-performance liquid chromatography, gas chromatography-mass spectrometry, and liquid chromatography-electrospray ionization/mass spectrometry analysis confirmed the degradation of MG by the formation of main metabolites 4-dimethylamino-benzophenone hydrate, N, N-dimethylaniline (N,N-dimethyl-benzenamine), and methylbenzaldehyde. Interestingly, it was found that rMnPH4 mediates hydroxyl radical attack on the central carbon of MG. Finally, rMnPH4 degraded MG resulted in the complete removal of its toxicity, which was checked under in vitro conditions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23604969</PMID><DateCompleted><Year>2014</Year><Month>05</Month><Day>19</Day></DateCompleted><DateRevised><Year>2013</Year><Month>10</Month><Day>31</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1559-0291</ISSN><JournalIssue CitedMedium="Internet"><Volume>171</Volume><Issue>5</Issue><PubDate><Year>2013</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Applied biochemistry and biotechnology</Title><ISOAbbreviation>Appl Biochem Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Manganese peroxidase h4 isozyme mediated degradation and detoxification of triarylmethane dye malachite green: optimization of decolorization by response surface methodology.</ArticleTitle><Pagination><MedlinePgn>1178-93</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12010-013-0220-4</ELocationID><Abstract><AbstractText>A cDNA encoding for manganese peroxidase isozyme H4 (MnPH4), isolated from Phanerochaete chrysosporium, was expressed in Pichia pastoris, under the control of alcohol oxidase I promoter. The recombinant MnPH4 was efficiently secreted onto media supplemented with hemin at a maximum concentration of 500 U/L, after which purified rMnPH4 was used to decolorize the triarylmethane dye malachite green (MG). Response surface methodology (RSM) was employed to optimize three different operational parameters for the decolorization of MG. RSM showed that the optimized variables of enzyme (0.662 U), MnSO4 (448 μM), and hydrogen peroxide (159 μM) decolorized 100 mg/L of MG completely at 3 h. Additionally, UV-VIS spectra, high-performance liquid chromatography, gas chromatography-mass spectrometry, and liquid chromatography-electrospray ionization/mass spectrometry analysis confirmed the degradation of MG by the formation of main metabolites 4-dimethylamino-benzophenone hydrate, N, N-dimethylaniline (N,N-dimethyl-benzenamine), and methylbenzaldehyde. Interestingly, it was found that rMnPH4 mediates hydroxyl radical attack on the central carbon of MG. Finally, rMnPH4 degraded MG resulted in the complete removal of its toxicity, which was checked under in vitro conditions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Saravanakumar</LastName><ForeName>Thiyagarajan</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Division of Biotechnology, College of Environmental and Bioresource Sciences, Chonbuk National University, Iksan, 570-752, South Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Palvannan</LastName><ForeName>Thayumanavan</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Dae-Hyuk</ForeName><Initials>DH</Initials></Author><Author ValidYN="Y"><LastName>Park</LastName><ForeName>Seung-Moon</ForeName><Initials>SM</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004396" MajorTopicYN="N">Coloring Agents</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012394" MajorTopicYN="N">Rosaniline Dyes</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>10</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>04</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>4</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>4</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>5</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23604969</ArticleId><ArticleId IdType="doi">10.1007/s12010-013-0220-4</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country></list><tree><noCountry><name sortKey="Kim, Dae Hyuk" sort="Kim, Dae Hyuk" uniqKey="Kim D" first="Dae-Hyuk" last="Kim">Dae-Hyuk Kim</name><name sortKey="Palvannan, Thayumanavan" sort="Palvannan, Thayumanavan" uniqKey="Palvannan T" first="Thayumanavan" last="Palvannan">Thayumanavan Palvannan</name><name sortKey="Park, Seung Moon" sort="Park, Seung Moon" uniqKey="Park S" first="Seung-Moon" last="Park">Seung-Moon Park</name></noCountry><country name="Corée du Sud"><noRegion><name sortKey="Saravanakumar, Thiyagarajan" sort="Saravanakumar, Thiyagarajan" uniqKey="Saravanakumar T" first="Thiyagarajan" last="Saravanakumar">Thiyagarajan Saravanakumar</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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