Production of ligninolytic enzymes for dye decolorization by cocultivation of white-rot fungi Pleurotus ostreatus and phanerochaete chrysosporium under solid-state fermentation.
Identifieur interne : 000985 ( Main/Corpus ); précédent : 000984; suivant : 000986Production of ligninolytic enzymes for dye decolorization by cocultivation of white-rot fungi Pleurotus ostreatus and phanerochaete chrysosporium under solid-state fermentation.
Auteurs : Pradeep Verma ; Datta MadamwarSource :
- Applied biochemistry and biotechnology [ 0273-2289 ]
English descriptors
- KwdEn :
- Biodegradation, Environmental (MeSH), Chemical Fractionation (methods), Color (MeSH), Coloring Agents (metabolism), Fermentation (MeSH), Industrial Waste (MeSH), Laccase (MeSH), Lignin (metabolism), Microscopy, Electron, Scanning (MeSH), Oxidoreductases (isolation & purification), Oxidoreductases (metabolism), Peroxidases (biosynthesis), Peroxidases (isolation & purification), Peroxidases (metabolism), Phanerochaete (enzymology), Pleurotus (enzymology), Substrate Specificity (MeSH).
- MESH :
- chemical , biosynthesis : Peroxidases.
- chemical , isolation & purification : Oxidoreductases, Peroxidases.
- chemical , metabolism : Coloring Agents, Lignin, Oxidoreductases, Peroxidases.
- enzymology : Phanerochaete, Pleurotus.
- methods : Chemical Fractionation.
- Biodegradation, Environmental, Color, Fermentation, Industrial Waste, Laccase, Microscopy, Electron, Scanning, Substrate Specificity.
Abstract
Lignocellulosic wastes such as neem hull, wheat bran, and sugarcane bagasse, available in abundance, are excellent substrates for the production of ligninolytic enzymes under solid-state fermentation by white-rot fungi. A ligninolytic enzyme system with high activity showing enhanced decomposition was obtained by cocultivation of Pleurotus ostreatus and Phanerochaete chrysosporium on combinations of lignocellulosic waste. Among the various substrate combinations examined, neem hull and wheat bran wastes gave the highest ligninolytic activity. A maximum production of laccase of 772 U/g and manganese peroxidase of 982 U/g was obtained on d 20 and lignin peroxidase of 656 U/g on d 25 at 28 +/- 1 degrees C under solid-state fermentation. All three enzymes thus obtained were partially purified by acetone fractionation and were exploited for decolorizing different types of acid and reactive dyes.
DOI: 10.1385/abab:102-103:1-6:109
PubMed: 12396115
Links to Exploration step
pubmed:12396115Le document en format XML
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A ligninolytic enzyme system with high activity showing enhanced decomposition was obtained by cocultivation of Pleurotus ostreatus and Phanerochaete chrysosporium on combinations of lignocellulosic waste. Among the various substrate combinations examined, neem hull and wheat bran wastes gave the highest ligninolytic activity. A maximum production of laccase of 772 U/g and manganese peroxidase of 982 U/g was obtained on d 20 and lignin peroxidase of 656 U/g on d 25 at 28 +/- 1 degrees C under solid-state fermentation. All three enzymes thus obtained were partially purified by acetone fractionation and were exploited for decolorizing different types of acid and reactive dyes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12396115</PMID><DateCompleted><Year>2003</Year><Month>05</Month><Day>21</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0273-2289</ISSN><JournalIssue CitedMedium="Print"><Volume>102-103</Volume><Issue>1-6</Issue><PubDate><MedlineDate>2002 Jul-Dec</MedlineDate></PubDate></JournalIssue><Title>Applied biochemistry and biotechnology</Title><ISOAbbreviation>Appl Biochem Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Production of ligninolytic enzymes for dye decolorization by cocultivation of white-rot fungi Pleurotus ostreatus and phanerochaete chrysosporium under solid-state fermentation.</ArticleTitle><Pagination><MedlinePgn>109-18</MedlinePgn></Pagination><Abstract><AbstractText>Lignocellulosic wastes such as neem hull, wheat bran, and sugarcane bagasse, available in abundance, are excellent substrates for the production of ligninolytic enzymes under solid-state fermentation by white-rot fungi. A ligninolytic enzyme system with high activity showing enhanced decomposition was obtained by cocultivation of Pleurotus ostreatus and Phanerochaete chrysosporium on combinations of lignocellulosic waste. Among the various substrate combinations examined, neem hull and wheat bran wastes gave the highest ligninolytic activity. A maximum production of laccase of 772 U/g and manganese peroxidase of 982 U/g was obtained on d 20 and lignin peroxidase of 656 U/g on d 25 at 28 +/- 1 degrees C under solid-state fermentation. All three enzymes thus obtained were partially purified by acetone fractionation and were exploited for decolorizing different types of acid and reactive dyes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Verma</LastName><ForeName>Pradeep</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Post-Graduate Department of Biosciences, Sardar Patel University, Gujarat, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Madamwar</LastName><ForeName>Datta</ForeName><Initials>D</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Appl Biochem Biotechnol</MedlineTA><NlmUniqueID>8208561</NlmUniqueID><ISSNLinking>0273-2289</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004396">Coloring Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007220">Industrial Waste</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance UI="D042845">Laccase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</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="D005591" MajorTopicYN="N">Chemical Fractionation</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003116" MajorTopicYN="N">Color</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004396" MajorTopicYN="N">Coloring Agents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005285" MajorTopicYN="N">Fermentation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007220" MajorTopicYN="N">Industrial Waste</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008855" MajorTopicYN="N">Microscopy, Electron, Scanning</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020076" MajorTopicYN="N">Pleurotus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>10</Month><Day>25</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>5</Month><Day>22</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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