Production of the Phanerochaete flavido-alba laccase in Aspergillus niger for synthetic dyes decolorization and biotransformation.
Identifieur interne : 000359 ( Main/Corpus ); précédent : 000358; suivant : 000360Production of the Phanerochaete flavido-alba laccase in Aspergillus niger for synthetic dyes decolorization and biotransformation.
Auteurs : Lamiae Benghazi ; Eric Record ; Antonio Suárez ; José A. Gomez-Vidal ; José Martínez ; Teresa De La RubiaSource :
- World journal of microbiology & biotechnology [ 1573-0972 ] ; 2014.
English descriptors
- KwdEn :
- Anthraquinones (metabolism), Aspergillus niger (genetics), Aspergillus niger (metabolism), Biotransformation (MeSH), Blotting, Western (MeSH), Coloring Agents (metabolism), Enzyme Stability (MeSH), Gene Expression (MeSH), Hydrogen-Ion Concentration (MeSH), Laccase (chemistry), Laccase (genetics), Laccase (isolation & purification), Laccase (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Rhodamines (metabolism), Sequence Analysis, Protein (MeSH), Solvents (MeSH).
- MESH :
- chemical , chemistry : Laccase, Recombinant Proteins.
- chemical , genetics : Laccase, Recombinant Proteins.
- chemical , isolation & purification : Laccase, Recombinant Proteins.
- chemical , metabolism : Anthraquinones, Coloring Agents, Laccase, Recombinant Proteins, Rhodamines.
- enzymology : Phanerochaete.
- genetics : Aspergillus niger, Phanerochaete.
- metabolism : Aspergillus niger.
- Biotransformation, Blotting, Western, Enzyme Stability, Gene Expression, Hydrogen-Ion Concentration, Sequence Analysis, Protein, Solvents.
Abstract
We investigated the expression of Phanerochaete flavido-alba laccase gene in Aspergillus niger and the physical and biochemical properties of the recombinant enzyme (rLac-LPFA) in order to test it for synthetic dye biotransformation. A. niger was able to produce high levels of active recombinant enzyme (30 mgL(-1)), whose identity was further confirmed by immunodetection using Western blot analysis and N-terminal sequencing. Interestingly, rLac-LPFA exhibited an improved stability at pH (2-9) and organic solvents tested. Furthermore, the percentage of decoloration and biotransformation of synthetic textile dyes, Remazol Brilliant Blue R (RBBR) and Acid Red 299 (NY1), was higher than for the native enzyme. Its high production, simple purification, high activity, stability and ability to transform textile dyes make rLac-LPFA a good candidate for industrial applications.
DOI: 10.1007/s11274-013-1440-z
PubMed: 23884844
Links to Exploration step
pubmed:23884844Le document en format XML
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Gomez-Vidal</name></author><author><name sortKey="Martinez, Jose" sort="Martinez, Jose" uniqKey="Martinez J" first="José" last="Martínez">José Martínez</name></author><author><name sortKey="De La Rubia, Teresa" sort="De La Rubia, Teresa" uniqKey="De La Rubia T" first="Teresa" last="De La Rubia">Teresa De La Rubia</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:23884844</idno><idno type="pmid">23884844</idno><idno type="doi">10.1007/s11274-013-1440-z</idno><idno type="wicri:Area/Main/Corpus">000359</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000359</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Production of the Phanerochaete flavido-alba laccase in Aspergillus niger for synthetic dyes decolorization and biotransformation.</title><author><name sortKey="Benghazi, Lamiae" sort="Benghazi, Lamiae" uniqKey="Benghazi L" first="Lamiae" last="Benghazi">Lamiae Benghazi</name><affiliation><nlm:affiliation>Department of Microbiology, Faculty of Pharmacy, University of Granada, Campus Cartuja, 18071, Granada, Spain.</nlm:affiliation></affiliation></author><author><name sortKey="Record, Eric" sort="Record, Eric" uniqKey="Record E" first="Eric" last="Record">Eric Record</name></author><author><name sortKey="Suarez, Antonio" sort="Suarez, Antonio" uniqKey="Suarez A" first="Antonio" last="Suárez">Antonio Suárez</name></author><author><name sortKey="Gomez Vidal, Jose A" sort="Gomez Vidal, Jose A" uniqKey="Gomez Vidal J" first="José A" last="Gomez-Vidal">José A. Gomez-Vidal</name></author><author><name sortKey="Martinez, Jose" sort="Martinez, Jose" uniqKey="Martinez J" first="José" last="Martínez">José Martínez</name></author><author><name sortKey="De La Rubia, Teresa" sort="De La Rubia, Teresa" uniqKey="De La Rubia T" first="Teresa" last="De La Rubia">Teresa De La Rubia</name></author></analytic><series><title level="j">World journal of microbiology & biotechnology</title><idno type="eISSN">1573-0972</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anthraquinones (metabolism)</term><term>Aspergillus niger (genetics)</term><term>Aspergillus niger (metabolism)</term><term>Biotransformation (MeSH)</term><term>Blotting, Western (MeSH)</term><term>Coloring Agents (metabolism)</term><term>Enzyme Stability (MeSH)</term><term>Gene Expression (MeSH)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Laccase (chemistry)</term><term>Laccase (genetics)</term><term>Laccase (isolation & purification)</term><term>Laccase (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (isolation & purification)</term><term>Recombinant Proteins (metabolism)</term><term>Rhodamines (metabolism)</term><term>Sequence Analysis, Protein (MeSH)</term><term>Solvents (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Laccase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Laccase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Laccase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Anthraquinones</term><term>Coloring Agents</term><term>Laccase</term><term>Recombinant Proteins</term><term>Rhodamines</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Aspergillus niger</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Aspergillus niger</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biotransformation</term><term>Blotting, Western</term><term>Enzyme Stability</term><term>Gene Expression</term><term>Hydrogen-Ion Concentration</term><term>Sequence Analysis, Protein</term><term>Solvents</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We investigated the expression of Phanerochaete flavido-alba laccase gene in Aspergillus niger and the physical and biochemical properties of the recombinant enzyme (rLac-LPFA) in order to test it for synthetic dye biotransformation. A. niger was able to produce high levels of active recombinant enzyme (30 mgL(-1)), whose identity was further confirmed by immunodetection using Western blot analysis and N-terminal sequencing. Interestingly, rLac-LPFA exhibited an improved stability at pH (2-9) and organic solvents tested. Furthermore, the percentage of decoloration and biotransformation of synthetic textile dyes, Remazol Brilliant Blue R (RBBR) and Acid Red 299 (NY1), was higher than for the native enzyme. Its high production, simple purification, high activity, stability and ability to transform textile dyes make rLac-LPFA a good candidate for industrial applications. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23884844</PMID><DateCompleted><Year>2014</Year><Month>08</Month><Day>26</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-0972</ISSN><JournalIssue CitedMedium="Internet"><Volume>30</Volume><Issue>1</Issue><PubDate><Year>2014</Year><Month>Jan</Month></PubDate></JournalIssue><Title>World journal of microbiology & biotechnology</Title><ISOAbbreviation>World J Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Production of the Phanerochaete flavido-alba laccase in Aspergillus niger for synthetic dyes decolorization and biotransformation.</ArticleTitle><Pagination><MedlinePgn>201-11</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s11274-013-1440-z</ELocationID><Abstract><AbstractText>We investigated the expression of Phanerochaete flavido-alba laccase gene in Aspergillus niger and the physical and biochemical properties of the recombinant enzyme (rLac-LPFA) in order to test it for synthetic dye biotransformation. A. niger was able to produce high levels of active recombinant enzyme (30 mgL(-1)), whose identity was further confirmed by immunodetection using Western blot analysis and N-terminal sequencing. Interestingly, rLac-LPFA exhibited an improved stability at pH (2-9) and organic solvents tested. Furthermore, the percentage of decoloration and biotransformation of synthetic textile dyes, Remazol Brilliant Blue R (RBBR) and Acid Red 299 (NY1), was higher than for the native enzyme. Its high production, simple purification, high activity, stability and ability to transform textile dyes make rLac-LPFA a good candidate for industrial applications. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Benghazi</LastName><ForeName>Lamiae</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Faculty of Pharmacy, University of Granada, Campus Cartuja, 18071, Granada, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Record</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Suárez</LastName><ForeName>Antonio</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Gomez-Vidal</LastName><ForeName>José A</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>José</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>de la 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Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012235">Rhodamines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012997">Solvents</NameOfSubstance></Chemical><Chemical><RegistryNumber>2609-88-3</RegistryNumber><NameOfSubstance UI="C022027">lissamine rhodamine B</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance UI="D042845">Laccase</NameOfSubstance></Chemical><Chemical><RegistryNumber>L51IMM9UP9</RegistryNumber><NameOfSubstance UI="C024758">Remazol Brilliant Blue R</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000880" MajorTopicYN="N">Anthraquinones</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001234" MajorTopicYN="N">Aspergillus niger</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001711" MajorTopicYN="N">Biotransformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004396" MajorTopicYN="N">Coloring Agents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</DescriptorName><QualifierName UI="Q000737" 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