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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<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>
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<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>
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<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>
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