Molecular cloning of the cDNA encoding laccase from Trametes versicolor and heterologous expression in Pichia methanolica
Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Guo, Mei [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2005 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2005 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer Berlin Heidelberg, 1984, 69(2005), 2 vom: Nov., Seite 178-183 |
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| Übergeordnetes Werk: |
volume:69 ; year:2005 ; number:2 ; month:11 ; pages:178-183 |
| Links: |
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| DOI / URN: |
10.1007/s00253-005-1985-3 |
|---|
| Katalog-ID: |
OLC2050704321 |
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| 520 | |a Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA and pMETαA and expressed in Pichia methanolica. The laccase activity obtained with the Saccharomyces cerevisiae α-factor signal peptide was found to be twofold higher than that obtained with the native secretion signal peptide. The extracellular laccase activity in recombinants with the α-factor signal peptide was 9.79 U $ ml^{−1} $. The presence of 0.2 mM copper was necessary for optimal activity of laccase. The expression level was favoured by lower cultivation temperature. The identity of the recombinant protein was further confirmed by immunodetection using Western blot analysis. As expected, the molecular mass of the mature laccase was 64.0 kDa, similar to that of the native form. | ||
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| 700 | 1 | |a Du, Lianxiang |4 aut | |
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10.1007/s00253-005-1985-3 doi (DE-627)OLC2050704321 (DE-He213)s00253-005-1985-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Guo, Mei verfasserin aut Molecular cloning of the cDNA encoding laccase from Trametes versicolor and heterologous expression in Pichia methanolica 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA and pMETαA and expressed in Pichia methanolica. The laccase activity obtained with the Saccharomyces cerevisiae α-factor signal peptide was found to be twofold higher than that obtained with the native secretion signal peptide. The extracellular laccase activity in recombinants with the α-factor signal peptide was 9.79 U $ ml^{−1} $. The presence of 0.2 mM copper was necessary for optimal activity of laccase. The expression level was favoured by lower cultivation temperature. The identity of the recombinant protein was further confirmed by immunodetection using Western blot analysis. As expected, the molecular mass of the mature laccase was 64.0 kDa, similar to that of the native form. Laccase Activity Blue Copper Secretion Signal Peptide Native Signal Peptide Lower Cultivation Temperature Lu, Fuping aut Pu, Jun aut Bai, Dongqing aut Du, Lianxiang aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 2 vom: Nov., Seite 178-183 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:2 month:11 pages:178-183 https://doi.org/10.1007/s00253-005-1985-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 2 11 178-183 |
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10.1007/s00253-005-1985-3 doi (DE-627)OLC2050704321 (DE-He213)s00253-005-1985-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Guo, Mei verfasserin aut Molecular cloning of the cDNA encoding laccase from Trametes versicolor and heterologous expression in Pichia methanolica 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA and pMETαA and expressed in Pichia methanolica. The laccase activity obtained with the Saccharomyces cerevisiae α-factor signal peptide was found to be twofold higher than that obtained with the native secretion signal peptide. The extracellular laccase activity in recombinants with the α-factor signal peptide was 9.79 U $ ml^{−1} $. The presence of 0.2 mM copper was necessary for optimal activity of laccase. The expression level was favoured by lower cultivation temperature. The identity of the recombinant protein was further confirmed by immunodetection using Western blot analysis. As expected, the molecular mass of the mature laccase was 64.0 kDa, similar to that of the native form. Laccase Activity Blue Copper Secretion Signal Peptide Native Signal Peptide Lower Cultivation Temperature Lu, Fuping aut Pu, Jun aut Bai, Dongqing aut Du, Lianxiang aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 2 vom: Nov., Seite 178-183 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:2 month:11 pages:178-183 https://doi.org/10.1007/s00253-005-1985-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 2 11 178-183 |
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10.1007/s00253-005-1985-3 doi (DE-627)OLC2050704321 (DE-He213)s00253-005-1985-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Guo, Mei verfasserin aut Molecular cloning of the cDNA encoding laccase from Trametes versicolor and heterologous expression in Pichia methanolica 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA and pMETαA and expressed in Pichia methanolica. The laccase activity obtained with the Saccharomyces cerevisiae α-factor signal peptide was found to be twofold higher than that obtained with the native secretion signal peptide. The extracellular laccase activity in recombinants with the α-factor signal peptide was 9.79 U $ ml^{−1} $. The presence of 0.2 mM copper was necessary for optimal activity of laccase. The expression level was favoured by lower cultivation temperature. The identity of the recombinant protein was further confirmed by immunodetection using Western blot analysis. As expected, the molecular mass of the mature laccase was 64.0 kDa, similar to that of the native form. Laccase Activity Blue Copper Secretion Signal Peptide Native Signal Peptide Lower Cultivation Temperature Lu, Fuping aut Pu, Jun aut Bai, Dongqing aut Du, Lianxiang aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 2 vom: Nov., Seite 178-183 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:2 month:11 pages:178-183 https://doi.org/10.1007/s00253-005-1985-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 2 11 178-183 |
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10.1007/s00253-005-1985-3 doi (DE-627)OLC2050704321 (DE-He213)s00253-005-1985-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Guo, Mei verfasserin aut Molecular cloning of the cDNA encoding laccase from Trametes versicolor and heterologous expression in Pichia methanolica 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA and pMETαA and expressed in Pichia methanolica. The laccase activity obtained with the Saccharomyces cerevisiae α-factor signal peptide was found to be twofold higher than that obtained with the native secretion signal peptide. The extracellular laccase activity in recombinants with the α-factor signal peptide was 9.79 U $ ml^{−1} $. The presence of 0.2 mM copper was necessary for optimal activity of laccase. The expression level was favoured by lower cultivation temperature. The identity of the recombinant protein was further confirmed by immunodetection using Western blot analysis. As expected, the molecular mass of the mature laccase was 64.0 kDa, similar to that of the native form. Laccase Activity Blue Copper Secretion Signal Peptide Native Signal Peptide Lower Cultivation Temperature Lu, Fuping aut Pu, Jun aut Bai, Dongqing aut Du, Lianxiang aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 2 vom: Nov., Seite 178-183 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:2 month:11 pages:178-183 https://doi.org/10.1007/s00253-005-1985-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 2 11 178-183 |
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10.1007/s00253-005-1985-3 doi (DE-627)OLC2050704321 (DE-He213)s00253-005-1985-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Guo, Mei verfasserin aut Molecular cloning of the cDNA encoding laccase from Trametes versicolor and heterologous expression in Pichia methanolica 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA and pMETαA and expressed in Pichia methanolica. The laccase activity obtained with the Saccharomyces cerevisiae α-factor signal peptide was found to be twofold higher than that obtained with the native secretion signal peptide. The extracellular laccase activity in recombinants with the α-factor signal peptide was 9.79 U $ ml^{−1} $. The presence of 0.2 mM copper was necessary for optimal activity of laccase. The expression level was favoured by lower cultivation temperature. The identity of the recombinant protein was further confirmed by immunodetection using Western blot analysis. As expected, the molecular mass of the mature laccase was 64.0 kDa, similar to that of the native form. Laccase Activity Blue Copper Secretion Signal Peptide Native Signal Peptide Lower Cultivation Temperature Lu, Fuping aut Pu, Jun aut Bai, Dongqing aut Du, Lianxiang aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 2 vom: Nov., Seite 178-183 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:2 month:11 pages:178-183 https://doi.org/10.1007/s00253-005-1985-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 2 11 178-183 |
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Enthalten in Applied microbiology and biotechnology 69(2005), 2 vom: Nov., Seite 178-183 volume:69 year:2005 number:2 month:11 pages:178-183 |
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Enthalten in Applied microbiology and biotechnology 69(2005), 2 vom: Nov., Seite 178-183 volume:69 year:2005 number:2 month:11 pages:178-183 |
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Guo, Mei @@aut@@ Lu, Fuping @@aut@@ Pu, Jun @@aut@@ Bai, Dongqing @@aut@@ Du, Lianxiang @@aut@@ |
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Molecular cloning of the cDNA encoding laccase from Trametes versicolor and heterologous expression in Pichia methanolica |
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Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA and pMETαA and expressed in Pichia methanolica. The laccase activity obtained with the Saccharomyces cerevisiae α-factor signal peptide was found to be twofold higher than that obtained with the native secretion signal peptide. The extracellular laccase activity in recombinants with the α-factor signal peptide was 9.79 U $ ml^{−1} $. The presence of 0.2 mM copper was necessary for optimal activity of laccase. The expression level was favoured by lower cultivation temperature. The identity of the recombinant protein was further confirmed by immunodetection using Western blot analysis. As expected, the molecular mass of the mature laccase was 64.0 kDa, similar to that of the native form. © Springer-Verlag 2005 |
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Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA and pMETαA and expressed in Pichia methanolica. The laccase activity obtained with the Saccharomyces cerevisiae α-factor signal peptide was found to be twofold higher than that obtained with the native secretion signal peptide. The extracellular laccase activity in recombinants with the α-factor signal peptide was 9.79 U $ ml^{−1} $. The presence of 0.2 mM copper was necessary for optimal activity of laccase. The expression level was favoured by lower cultivation temperature. The identity of the recombinant protein was further confirmed by immunodetection using Western blot analysis. As expected, the molecular mass of the mature laccase was 64.0 kDa, similar to that of the native form. © Springer-Verlag 2005 |
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Abstract A cDNA encoding for laccase was isolated from the ligninolytic fungus Trametes versicolor by RNA-PCR. The cDNA corresponds to the gene Lcc1, which encodes a laccase isoenzyme of 498 amino acid residues preceded by a 22-residue signal peptide. The Lcc1 cDNA was cloned into the vectors pMETA and pMETαA and expressed in Pichia methanolica. The laccase activity obtained with the Saccharomyces cerevisiae α-factor signal peptide was found to be twofold higher than that obtained with the native secretion signal peptide. The extracellular laccase activity in recombinants with the α-factor signal peptide was 9.79 U $ ml^{−1} $. The presence of 0.2 mM copper was necessary for optimal activity of laccase. The expression level was favoured by lower cultivation temperature. The identity of the recombinant protein was further confirmed by immunodetection using Western blot analysis. As expected, the molecular mass of the mature laccase was 64.0 kDa, similar to that of the native form. © Springer-Verlag 2005 |
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