Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach
Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms we...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Tutuncu, Havva Esra [verfasserIn] Balci, Nurgul [verfasserIn] Tuter, Melek [verfasserIn] Karaguler, Nevin Gul [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Extremophiles - Springer-Verlag, 2001, 23(2019), 5 vom: 01. Juni, Seite 507-520 |
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| Übergeordnetes Werk: |
volume:23 ; year:2019 ; number:5 ; day:01 ; month:06 ; pages:507-520 |
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| DOI / URN: |
10.1007/s00792-019-01103-w |
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| 520 | |a Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms were used for polymerase chain reaction (PCR) and a whole gene was identified by genome walking. The gene was composed of 783 bp, which corresponds to 260 amino acids with a molecular weight of 28.2 kDa. The deduced amino acid sequence best matched with the esterase from Halomonas gudaonensis with an identity of 91%. Recombinantly expressed enzyme exhibited maximum activity towards pNP-hexanoate with a kcat value of 12.30 $ s^{−1} $. The optimum pH and temperature of the enzyme were found as 9 and 30 °C, respectively. The effects of NaCl, solvents, metal ions, detergents and enzyme inhibitors were also studied. In conclusion, a novel enzyme, named as hypersaline lake “Acıgöl” esterase (hAGEst), was identified by sequence-based metagenomics. The high expression level, the ability to maintain activity at cold temperatures and tolerance to DMSO and metal ions are the most outstanding properties of the hAGEst. | ||
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10.1007/s00792-019-01103-w doi (DE-627)SPR007867689 (SPR)s00792-019-01103-w-e DE-627 ger DE-627 rakwb eng Tutuncu, Havva Esra verfasserin aut Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms were used for polymerase chain reaction (PCR) and a whole gene was identified by genome walking. The gene was composed of 783 bp, which corresponds to 260 amino acids with a molecular weight of 28.2 kDa. The deduced amino acid sequence best matched with the esterase from Halomonas gudaonensis with an identity of 91%. Recombinantly expressed enzyme exhibited maximum activity towards pNP-hexanoate with a kcat value of 12.30 $ s^{−1} $. The optimum pH and temperature of the enzyme were found as 9 and 30 °C, respectively. The effects of NaCl, solvents, metal ions, detergents and enzyme inhibitors were also studied. In conclusion, a novel enzyme, named as hypersaline lake “Acıgöl” esterase (hAGEst), was identified by sequence-based metagenomics. The high expression level, the ability to maintain activity at cold temperatures and tolerance to DMSO and metal ions are the most outstanding properties of the hAGEst. Degenerate PCR (dpeaa)DE-He213 Esterase (dpeaa)DE-He213 Genome walking (dpeaa)DE-He213 Halophiles (dpeaa)DE-He213 Lake Acigöl (dpeaa)DE-He213 Metagenomics (dpeaa)DE-He213 Balci, Nurgul verfasserin aut Tuter, Melek verfasserin aut Karaguler, Nevin Gul verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 23(2019), 5 vom: 01. Juni, Seite 507-520 (DE-627)SPR007852657 nnns volume:23 year:2019 number:5 day:01 month:06 pages:507-520 https://dx.doi.org/10.1007/s00792-019-01103-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 23 2019 5 01 06 507-520 |
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10.1007/s00792-019-01103-w doi (DE-627)SPR007867689 (SPR)s00792-019-01103-w-e DE-627 ger DE-627 rakwb eng Tutuncu, Havva Esra verfasserin aut Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms were used for polymerase chain reaction (PCR) and a whole gene was identified by genome walking. The gene was composed of 783 bp, which corresponds to 260 amino acids with a molecular weight of 28.2 kDa. The deduced amino acid sequence best matched with the esterase from Halomonas gudaonensis with an identity of 91%. Recombinantly expressed enzyme exhibited maximum activity towards pNP-hexanoate with a kcat value of 12.30 $ s^{−1} $. The optimum pH and temperature of the enzyme were found as 9 and 30 °C, respectively. The effects of NaCl, solvents, metal ions, detergents and enzyme inhibitors were also studied. In conclusion, a novel enzyme, named as hypersaline lake “Acıgöl” esterase (hAGEst), was identified by sequence-based metagenomics. The high expression level, the ability to maintain activity at cold temperatures and tolerance to DMSO and metal ions are the most outstanding properties of the hAGEst. Degenerate PCR (dpeaa)DE-He213 Esterase (dpeaa)DE-He213 Genome walking (dpeaa)DE-He213 Halophiles (dpeaa)DE-He213 Lake Acigöl (dpeaa)DE-He213 Metagenomics (dpeaa)DE-He213 Balci, Nurgul verfasserin aut Tuter, Melek verfasserin aut Karaguler, Nevin Gul verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 23(2019), 5 vom: 01. Juni, Seite 507-520 (DE-627)SPR007852657 nnns volume:23 year:2019 number:5 day:01 month:06 pages:507-520 https://dx.doi.org/10.1007/s00792-019-01103-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 23 2019 5 01 06 507-520 |
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10.1007/s00792-019-01103-w doi (DE-627)SPR007867689 (SPR)s00792-019-01103-w-e DE-627 ger DE-627 rakwb eng Tutuncu, Havva Esra verfasserin aut Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms were used for polymerase chain reaction (PCR) and a whole gene was identified by genome walking. The gene was composed of 783 bp, which corresponds to 260 amino acids with a molecular weight of 28.2 kDa. The deduced amino acid sequence best matched with the esterase from Halomonas gudaonensis with an identity of 91%. Recombinantly expressed enzyme exhibited maximum activity towards pNP-hexanoate with a kcat value of 12.30 $ s^{−1} $. The optimum pH and temperature of the enzyme were found as 9 and 30 °C, respectively. The effects of NaCl, solvents, metal ions, detergents and enzyme inhibitors were also studied. In conclusion, a novel enzyme, named as hypersaline lake “Acıgöl” esterase (hAGEst), was identified by sequence-based metagenomics. The high expression level, the ability to maintain activity at cold temperatures and tolerance to DMSO and metal ions are the most outstanding properties of the hAGEst. Degenerate PCR (dpeaa)DE-He213 Esterase (dpeaa)DE-He213 Genome walking (dpeaa)DE-He213 Halophiles (dpeaa)DE-He213 Lake Acigöl (dpeaa)DE-He213 Metagenomics (dpeaa)DE-He213 Balci, Nurgul verfasserin aut Tuter, Melek verfasserin aut Karaguler, Nevin Gul verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 23(2019), 5 vom: 01. Juni, Seite 507-520 (DE-627)SPR007852657 nnns volume:23 year:2019 number:5 day:01 month:06 pages:507-520 https://dx.doi.org/10.1007/s00792-019-01103-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 23 2019 5 01 06 507-520 |
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10.1007/s00792-019-01103-w doi (DE-627)SPR007867689 (SPR)s00792-019-01103-w-e DE-627 ger DE-627 rakwb eng Tutuncu, Havva Esra verfasserin aut Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms were used for polymerase chain reaction (PCR) and a whole gene was identified by genome walking. The gene was composed of 783 bp, which corresponds to 260 amino acids with a molecular weight of 28.2 kDa. The deduced amino acid sequence best matched with the esterase from Halomonas gudaonensis with an identity of 91%. Recombinantly expressed enzyme exhibited maximum activity towards pNP-hexanoate with a kcat value of 12.30 $ s^{−1} $. The optimum pH and temperature of the enzyme were found as 9 and 30 °C, respectively. The effects of NaCl, solvents, metal ions, detergents and enzyme inhibitors were also studied. In conclusion, a novel enzyme, named as hypersaline lake “Acıgöl” esterase (hAGEst), was identified by sequence-based metagenomics. The high expression level, the ability to maintain activity at cold temperatures and tolerance to DMSO and metal ions are the most outstanding properties of the hAGEst. Degenerate PCR (dpeaa)DE-He213 Esterase (dpeaa)DE-He213 Genome walking (dpeaa)DE-He213 Halophiles (dpeaa)DE-He213 Lake Acigöl (dpeaa)DE-He213 Metagenomics (dpeaa)DE-He213 Balci, Nurgul verfasserin aut Tuter, Melek verfasserin aut Karaguler, Nevin Gul verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 23(2019), 5 vom: 01. Juni, Seite 507-520 (DE-627)SPR007852657 nnns volume:23 year:2019 number:5 day:01 month:06 pages:507-520 https://dx.doi.org/10.1007/s00792-019-01103-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 23 2019 5 01 06 507-520 |
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10.1007/s00792-019-01103-w doi (DE-627)SPR007867689 (SPR)s00792-019-01103-w-e DE-627 ger DE-627 rakwb eng Tutuncu, Havva Esra verfasserin aut Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms were used for polymerase chain reaction (PCR) and a whole gene was identified by genome walking. The gene was composed of 783 bp, which corresponds to 260 amino acids with a molecular weight of 28.2 kDa. The deduced amino acid sequence best matched with the esterase from Halomonas gudaonensis with an identity of 91%. Recombinantly expressed enzyme exhibited maximum activity towards pNP-hexanoate with a kcat value of 12.30 $ s^{−1} $. The optimum pH and temperature of the enzyme were found as 9 and 30 °C, respectively. The effects of NaCl, solvents, metal ions, detergents and enzyme inhibitors were also studied. In conclusion, a novel enzyme, named as hypersaline lake “Acıgöl” esterase (hAGEst), was identified by sequence-based metagenomics. The high expression level, the ability to maintain activity at cold temperatures and tolerance to DMSO and metal ions are the most outstanding properties of the hAGEst. Degenerate PCR (dpeaa)DE-He213 Esterase (dpeaa)DE-He213 Genome walking (dpeaa)DE-He213 Halophiles (dpeaa)DE-He213 Lake Acigöl (dpeaa)DE-He213 Metagenomics (dpeaa)DE-He213 Balci, Nurgul verfasserin aut Tuter, Melek verfasserin aut Karaguler, Nevin Gul verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 23(2019), 5 vom: 01. Juni, Seite 507-520 (DE-627)SPR007852657 nnns volume:23 year:2019 number:5 day:01 month:06 pages:507-520 https://dx.doi.org/10.1007/s00792-019-01103-w lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 23 2019 5 01 06 507-520 |
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Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach |
| abstract |
Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms were used for polymerase chain reaction (PCR) and a whole gene was identified by genome walking. The gene was composed of 783 bp, which corresponds to 260 amino acids with a molecular weight of 28.2 kDa. The deduced amino acid sequence best matched with the esterase from Halomonas gudaonensis with an identity of 91%. Recombinantly expressed enzyme exhibited maximum activity towards pNP-hexanoate with a kcat value of 12.30 $ s^{−1} $. The optimum pH and temperature of the enzyme were found as 9 and 30 °C, respectively. The effects of NaCl, solvents, metal ions, detergents and enzyme inhibitors were also studied. In conclusion, a novel enzyme, named as hypersaline lake “Acıgöl” esterase (hAGEst), was identified by sequence-based metagenomics. The high expression level, the ability to maintain activity at cold temperatures and tolerance to DMSO and metal ions are the most outstanding properties of the hAGEst. |
| abstractGer |
Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms were used for polymerase chain reaction (PCR) and a whole gene was identified by genome walking. The gene was composed of 783 bp, which corresponds to 260 amino acids with a molecular weight of 28.2 kDa. The deduced amino acid sequence best matched with the esterase from Halomonas gudaonensis with an identity of 91%. Recombinantly expressed enzyme exhibited maximum activity towards pNP-hexanoate with a kcat value of 12.30 $ s^{−1} $. The optimum pH and temperature of the enzyme were found as 9 and 30 °C, respectively. The effects of NaCl, solvents, metal ions, detergents and enzyme inhibitors were also studied. In conclusion, a novel enzyme, named as hypersaline lake “Acıgöl” esterase (hAGEst), was identified by sequence-based metagenomics. The high expression level, the ability to maintain activity at cold temperatures and tolerance to DMSO and metal ions are the most outstanding properties of the hAGEst. |
| abstract_unstemmed |
Abstract The aim of this study was to isolate a novel esterase from a hypersaline lake by sequence-based metagenomics. The metagenomic DNA was isolated from the enriched hypersaline lake sediment. Degenerate primers targeting the conserved regions of lipolytic enzymes of halophilic microorganisms were used for polymerase chain reaction (PCR) and a whole gene was identified by genome walking. The gene was composed of 783 bp, which corresponds to 260 amino acids with a molecular weight of 28.2 kDa. The deduced amino acid sequence best matched with the esterase from Halomonas gudaonensis with an identity of 91%. Recombinantly expressed enzyme exhibited maximum activity towards pNP-hexanoate with a kcat value of 12.30 $ s^{−1} $. The optimum pH and temperature of the enzyme were found as 9 and 30 °C, respectively. The effects of NaCl, solvents, metal ions, detergents and enzyme inhibitors were also studied. In conclusion, a novel enzyme, named as hypersaline lake “Acıgöl” esterase (hAGEst), was identified by sequence-based metagenomics. The high expression level, the ability to maintain activity at cold temperatures and tolerance to DMSO and metal ions are the most outstanding properties of the hAGEst. |
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GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER |
| container_issue |
5 |
| title_short |
Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach |
| url |
https://dx.doi.org/10.1007/s00792-019-01103-w |
| remote_bool |
true |
| author2 |
Balci, Nurgul Tuter, Melek Karaguler, Nevin Gul |
| author2Str |
Balci, Nurgul Tuter, Melek Karaguler, Nevin Gul |
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SPR007852657 |
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| doi_str |
10.1007/s00792-019-01103-w |
| up_date |
2024-07-03T15:45:30.836Z |
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