Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7
Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Guo, Hailun [verfasserIn] Zhang, Yan [verfasserIn] Shao, Yanchun [verfasserIn] Chen, Wanping [verfasserIn] Chen, Fusheng [verfasserIn] Li, Mu [verfasserIn] |
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E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016 |
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Enthalten in: Extremophiles - Springer-Verlag, 2001, 20(2016), 4 vom: 21. Mai, Seite 451-459 |
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volume:20 ; year:2016 ; number:4 ; day:21 ; month:05 ; pages:451-459 |
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10.1007/s00792-016-0835-9 |
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| 520 | |a Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif $ Gly^{173} $-Xaa-$ Ser^{175} $-Xaa-$ Gly^{177} $ that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4–10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184–216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase. | ||
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10.1007/s00792-016-0835-9 doi (DE-627)SPR007864752 (SPR)s00792-016-0835-9-e DE-627 ger DE-627 rakwb eng Guo, Hailun verfasserin aut Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif $ Gly^{173} $-Xaa-$ Ser^{175} $-Xaa-$ Gly^{177} $ that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4–10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184–216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase. Esterase (dpeaa)DE-He213 Gene cloning and expression (dpeaa)DE-He213 Cold active (dpeaa)DE-He213 Industrial applications (dpeaa)DE-He213 Zhang, Yan verfasserin aut Shao, Yanchun verfasserin aut Chen, Wanping verfasserin aut Chen, Fusheng verfasserin aut Li, Mu verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 20(2016), 4 vom: 21. Mai, Seite 451-459 (DE-627)SPR007852657 nnns volume:20 year:2016 number:4 day:21 month:05 pages:451-459 https://dx.doi.org/10.1007/s00792-016-0835-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 20 2016 4 21 05 451-459 |
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10.1007/s00792-016-0835-9 doi (DE-627)SPR007864752 (SPR)s00792-016-0835-9-e DE-627 ger DE-627 rakwb eng Guo, Hailun verfasserin aut Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif $ Gly^{173} $-Xaa-$ Ser^{175} $-Xaa-$ Gly^{177} $ that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4–10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184–216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase. Esterase (dpeaa)DE-He213 Gene cloning and expression (dpeaa)DE-He213 Cold active (dpeaa)DE-He213 Industrial applications (dpeaa)DE-He213 Zhang, Yan verfasserin aut Shao, Yanchun verfasserin aut Chen, Wanping verfasserin aut Chen, Fusheng verfasserin aut Li, Mu verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 20(2016), 4 vom: 21. Mai, Seite 451-459 (DE-627)SPR007852657 nnns volume:20 year:2016 number:4 day:21 month:05 pages:451-459 https://dx.doi.org/10.1007/s00792-016-0835-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 20 2016 4 21 05 451-459 |
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10.1007/s00792-016-0835-9 doi (DE-627)SPR007864752 (SPR)s00792-016-0835-9-e DE-627 ger DE-627 rakwb eng Guo, Hailun verfasserin aut Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif $ Gly^{173} $-Xaa-$ Ser^{175} $-Xaa-$ Gly^{177} $ that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4–10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184–216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase. Esterase (dpeaa)DE-He213 Gene cloning and expression (dpeaa)DE-He213 Cold active (dpeaa)DE-He213 Industrial applications (dpeaa)DE-He213 Zhang, Yan verfasserin aut Shao, Yanchun verfasserin aut Chen, Wanping verfasserin aut Chen, Fusheng verfasserin aut Li, Mu verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 20(2016), 4 vom: 21. Mai, Seite 451-459 (DE-627)SPR007852657 nnns volume:20 year:2016 number:4 day:21 month:05 pages:451-459 https://dx.doi.org/10.1007/s00792-016-0835-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 20 2016 4 21 05 451-459 |
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10.1007/s00792-016-0835-9 doi (DE-627)SPR007864752 (SPR)s00792-016-0835-9-e DE-627 ger DE-627 rakwb eng Guo, Hailun verfasserin aut Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif $ Gly^{173} $-Xaa-$ Ser^{175} $-Xaa-$ Gly^{177} $ that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4–10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184–216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase. Esterase (dpeaa)DE-He213 Gene cloning and expression (dpeaa)DE-He213 Cold active (dpeaa)DE-He213 Industrial applications (dpeaa)DE-He213 Zhang, Yan verfasserin aut Shao, Yanchun verfasserin aut Chen, Wanping verfasserin aut Chen, Fusheng verfasserin aut Li, Mu verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 20(2016), 4 vom: 21. Mai, Seite 451-459 (DE-627)SPR007852657 nnns volume:20 year:2016 number:4 day:21 month:05 pages:451-459 https://dx.doi.org/10.1007/s00792-016-0835-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 20 2016 4 21 05 451-459 |
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10.1007/s00792-016-0835-9 doi (DE-627)SPR007864752 (SPR)s00792-016-0835-9-e DE-627 ger DE-627 rakwb eng Guo, Hailun verfasserin aut Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif $ Gly^{173} $-Xaa-$ Ser^{175} $-Xaa-$ Gly^{177} $ that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4–10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184–216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase. Esterase (dpeaa)DE-He213 Gene cloning and expression (dpeaa)DE-He213 Cold active (dpeaa)DE-He213 Industrial applications (dpeaa)DE-He213 Zhang, Yan verfasserin aut Shao, Yanchun verfasserin aut Chen, Wanping verfasserin aut Chen, Fusheng verfasserin aut Li, Mu verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 20(2016), 4 vom: 21. Mai, Seite 451-459 (DE-627)SPR007852657 nnns volume:20 year:2016 number:4 day:21 month:05 pages:451-459 https://dx.doi.org/10.1007/s00792-016-0835-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 20 2016 4 21 05 451-459 |
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Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7 |
| abstract |
Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif $ Gly^{173} $-Xaa-$ Ser^{175} $-Xaa-$ Gly^{177} $ that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4–10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184–216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase. |
| abstractGer |
Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif $ Gly^{173} $-Xaa-$ Ser^{175} $-Xaa-$ Gly^{177} $ that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4–10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184–216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase. |
| abstract_unstemmed |
Abstract Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif $ Gly^{173} $-Xaa-$ Ser^{175} $-Xaa-$ Gly^{177} $ that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4–10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184–216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase. |
| collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER |
| container_issue |
4 |
| title_short |
Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7 |
| url |
https://dx.doi.org/10.1007/s00792-016-0835-9 |
| remote_bool |
true |
| author2 |
Zhang, Yan Shao, Yanchun Chen, Wanping Chen, Fusheng Li, Mu |
| author2Str |
Zhang, Yan Shao, Yanchun Chen, Wanping Chen, Fusheng Li, Mu |
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SPR007852657 |
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| doi_str |
10.1007/s00792-016-0835-9 |
| up_date |
2024-07-03T15:44:30.383Z |
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