Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007
A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Yuan, Dongjuan [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016 |
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| Rechteinformationen: |
Nutzungsrecht: © 2014 International Union of Biochemistry and Molecular Biology, Inc. |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Biotechnology & applied biochemistry - Hoboken, NJ : Wiley-Blackwell, 1986, 63(2016), 1, Seite 41-50 |
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| Übergeordnetes Werk: |
volume:63 ; year:2016 ; number:1 ; pages:41-50 |
| Links: |
|---|
| DOI / URN: |
10.1002/bab.1338 |
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| 520 | |a A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application. | ||
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| 650 | 4 | |a sp. strain W007 | |
| 650 | 4 | |a thermostable lipase | |
| 650 | 4 | |a pairwise alignment | |
| 650 | 4 | |a triacylglycerol lipase | |
| 650 | 4 | |a Streptomyces | |
| 700 | 1 | |a Xin, Ruipu |4 oth | |
| 700 | 1 | |a Wang, Yonghua |4 oth | |
| 700 | 1 | |a Lan, Dongming |4 oth | |
| 700 | 1 | |a Yang, Bo |4 oth | |
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10.1002/bab.1338 doi PQ20160307 (DE-627)OLC197195490X (DE-599)GBVOLC197195490X (PRQ)p1138-482b40afbdd1514bdc777922cdae601213f8e8c6bcf5d7fa30097909facff2020 (KEY)0100570720160000063000100041screeningandcharacterizationofathermostablelipasef DE-627 ger DE-627 rakwb eng 570 ZDB Yuan, Dongjuan verfasserin aut Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application. Nutzungsrecht: © 2014 International Union of Biochemistry and Molecular Biology, Inc. sp. strain W007 thermostable lipase pairwise alignment triacylglycerol lipase Streptomyces Xin, Ruipu oth Wang, Yonghua oth Lan, Dongming oth Yang, Bo oth Enthalten in Biotechnology & applied biochemistry Hoboken, NJ : Wiley-Blackwell, 1986 63(2016), 1, Seite 41-50 (DE-627)130679461 (DE-600)883433-7 (DE-576)018288111 0885-4513 nnns volume:63 year:2016 number:1 pages:41-50 http://dx.doi.org/10.1002/bab.1338 Volltext http://onlinelibrary.wiley.com/doi/10.1002/bab.1338/abstract http://www.ncbi.nlm.nih.gov/pubmed/25639796 http://search.proquest.com/docview/1764811408 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4310 AR 63 2016 1 41-50 |
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10.1002/bab.1338 doi PQ20160307 (DE-627)OLC197195490X (DE-599)GBVOLC197195490X (PRQ)p1138-482b40afbdd1514bdc777922cdae601213f8e8c6bcf5d7fa30097909facff2020 (KEY)0100570720160000063000100041screeningandcharacterizationofathermostablelipasef DE-627 ger DE-627 rakwb eng 570 ZDB Yuan, Dongjuan verfasserin aut Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application. Nutzungsrecht: © 2014 International Union of Biochemistry and Molecular Biology, Inc. sp. strain W007 thermostable lipase pairwise alignment triacylglycerol lipase Streptomyces Xin, Ruipu oth Wang, Yonghua oth Lan, Dongming oth Yang, Bo oth Enthalten in Biotechnology & applied biochemistry Hoboken, NJ : Wiley-Blackwell, 1986 63(2016), 1, Seite 41-50 (DE-627)130679461 (DE-600)883433-7 (DE-576)018288111 0885-4513 nnns volume:63 year:2016 number:1 pages:41-50 http://dx.doi.org/10.1002/bab.1338 Volltext http://onlinelibrary.wiley.com/doi/10.1002/bab.1338/abstract http://www.ncbi.nlm.nih.gov/pubmed/25639796 http://search.proquest.com/docview/1764811408 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4310 AR 63 2016 1 41-50 |
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10.1002/bab.1338 doi PQ20160307 (DE-627)OLC197195490X (DE-599)GBVOLC197195490X (PRQ)p1138-482b40afbdd1514bdc777922cdae601213f8e8c6bcf5d7fa30097909facff2020 (KEY)0100570720160000063000100041screeningandcharacterizationofathermostablelipasef DE-627 ger DE-627 rakwb eng 570 ZDB Yuan, Dongjuan verfasserin aut Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application. Nutzungsrecht: © 2014 International Union of Biochemistry and Molecular Biology, Inc. sp. strain W007 thermostable lipase pairwise alignment triacylglycerol lipase Streptomyces Xin, Ruipu oth Wang, Yonghua oth Lan, Dongming oth Yang, Bo oth Enthalten in Biotechnology & applied biochemistry Hoboken, NJ : Wiley-Blackwell, 1986 63(2016), 1, Seite 41-50 (DE-627)130679461 (DE-600)883433-7 (DE-576)018288111 0885-4513 nnns volume:63 year:2016 number:1 pages:41-50 http://dx.doi.org/10.1002/bab.1338 Volltext http://onlinelibrary.wiley.com/doi/10.1002/bab.1338/abstract http://www.ncbi.nlm.nih.gov/pubmed/25639796 http://search.proquest.com/docview/1764811408 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4310 AR 63 2016 1 41-50 |
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10.1002/bab.1338 doi PQ20160307 (DE-627)OLC197195490X (DE-599)GBVOLC197195490X (PRQ)p1138-482b40afbdd1514bdc777922cdae601213f8e8c6bcf5d7fa30097909facff2020 (KEY)0100570720160000063000100041screeningandcharacterizationofathermostablelipasef DE-627 ger DE-627 rakwb eng 570 ZDB Yuan, Dongjuan verfasserin aut Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application. Nutzungsrecht: © 2014 International Union of Biochemistry and Molecular Biology, Inc. sp. strain W007 thermostable lipase pairwise alignment triacylglycerol lipase Streptomyces Xin, Ruipu oth Wang, Yonghua oth Lan, Dongming oth Yang, Bo oth Enthalten in Biotechnology & applied biochemistry Hoboken, NJ : Wiley-Blackwell, 1986 63(2016), 1, Seite 41-50 (DE-627)130679461 (DE-600)883433-7 (DE-576)018288111 0885-4513 nnns volume:63 year:2016 number:1 pages:41-50 http://dx.doi.org/10.1002/bab.1338 Volltext http://onlinelibrary.wiley.com/doi/10.1002/bab.1338/abstract http://www.ncbi.nlm.nih.gov/pubmed/25639796 http://search.proquest.com/docview/1764811408 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4310 AR 63 2016 1 41-50 |
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10.1002/bab.1338 doi PQ20160307 (DE-627)OLC197195490X (DE-599)GBVOLC197195490X (PRQ)p1138-482b40afbdd1514bdc777922cdae601213f8e8c6bcf5d7fa30097909facff2020 (KEY)0100570720160000063000100041screeningandcharacterizationofathermostablelipasef DE-627 ger DE-627 rakwb eng 570 ZDB Yuan, Dongjuan verfasserin aut Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application. Nutzungsrecht: © 2014 International Union of Biochemistry and Molecular Biology, Inc. sp. strain W007 thermostable lipase pairwise alignment triacylglycerol lipase Streptomyces Xin, Ruipu oth Wang, Yonghua oth Lan, Dongming oth Yang, Bo oth Enthalten in Biotechnology & applied biochemistry Hoboken, NJ : Wiley-Blackwell, 1986 63(2016), 1, Seite 41-50 (DE-627)130679461 (DE-600)883433-7 (DE-576)018288111 0885-4513 nnns volume:63 year:2016 number:1 pages:41-50 http://dx.doi.org/10.1002/bab.1338 Volltext http://onlinelibrary.wiley.com/doi/10.1002/bab.1338/abstract http://www.ncbi.nlm.nih.gov/pubmed/25639796 http://search.proquest.com/docview/1764811408 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4012 GBV_ILN_4310 AR 63 2016 1 41-50 |
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Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. 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screening and characterization of a thermostable lipase from marine streptomyces sp. strain w007 |
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Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007 |
| abstract |
A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application. |
| abstractGer |
A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application. |
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A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X‐33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well‐characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0–9.0. It was stable and retained about 90% of initial activity in the presence of Cu 2+ , Ca 2+ , Ni 2+ , and Mg 2+ , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application. |
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Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007 |
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