Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity
Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Li, Xiaolei [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2009 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2009 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 85(2009), 6 vom: 26. Aug., Seite 1821-1830 |
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| Übergeordnetes Werk: |
volume:85 ; year:2009 ; number:6 ; day:26 ; month:08 ; pages:1821-1830 |
| Links: |
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| DOI / URN: |
10.1007/s00253-009-2190-6 |
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| Katalog-ID: |
OLC2050726422 |
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| 245 | 1 | 0 | |a Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity |
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| 520 | |a Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. TfMA activity increased to 136% in the presence of 5 mM $ CaCl_{2} $. Maximal activity was measured toward γ-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one α-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase. | ||
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| 650 | 4 | |a Hyperthermophile | |
| 700 | 1 | |a Li, Dan |4 aut | |
| 700 | 1 | |a Yin, Yongguang |4 aut | |
| 700 | 1 | |a Park, Kwan-Hwa |4 aut | |
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10.1007/s00253-009-2190-6 doi (DE-627)OLC2050726422 (DE-He213)s00253-009-2190-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Li, Xiaolei verfasserin aut Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. TfMA activity increased to 136% in the presence of 5 mM $ CaCl_{2} $. Maximal activity was measured toward γ-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one α-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase. Maltogenic amylase Cyclodextrin Archaea Hyperthermophile Li, Dan aut Yin, Yongguang aut Park, Kwan-Hwa aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 85(2009), 6 vom: 26. Aug., Seite 1821-1830 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:85 year:2009 number:6 day:26 month:08 pages:1821-1830 https://doi.org/10.1007/s00253-009-2190-6 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_21 GBV_ILN_23 GBV_ILN_40 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_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 85 2009 6 26 08 1821-1830 |
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10.1007/s00253-009-2190-6 doi (DE-627)OLC2050726422 (DE-He213)s00253-009-2190-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Li, Xiaolei verfasserin aut Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. TfMA activity increased to 136% in the presence of 5 mM $ CaCl_{2} $. Maximal activity was measured toward γ-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one α-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase. Maltogenic amylase Cyclodextrin Archaea Hyperthermophile Li, Dan aut Yin, Yongguang aut Park, Kwan-Hwa aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 85(2009), 6 vom: 26. Aug., Seite 1821-1830 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:85 year:2009 number:6 day:26 month:08 pages:1821-1830 https://doi.org/10.1007/s00253-009-2190-6 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_21 GBV_ILN_23 GBV_ILN_40 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_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 85 2009 6 26 08 1821-1830 |
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10.1007/s00253-009-2190-6 doi (DE-627)OLC2050726422 (DE-He213)s00253-009-2190-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Li, Xiaolei verfasserin aut Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. TfMA activity increased to 136% in the presence of 5 mM $ CaCl_{2} $. Maximal activity was measured toward γ-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one α-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase. Maltogenic amylase Cyclodextrin Archaea Hyperthermophile Li, Dan aut Yin, Yongguang aut Park, Kwan-Hwa aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 85(2009), 6 vom: 26. Aug., Seite 1821-1830 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:85 year:2009 number:6 day:26 month:08 pages:1821-1830 https://doi.org/10.1007/s00253-009-2190-6 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_21 GBV_ILN_23 GBV_ILN_40 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_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 85 2009 6 26 08 1821-1830 |
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10.1007/s00253-009-2190-6 doi (DE-627)OLC2050726422 (DE-He213)s00253-009-2190-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Li, Xiaolei verfasserin aut Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. TfMA activity increased to 136% in the presence of 5 mM $ CaCl_{2} $. Maximal activity was measured toward γ-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one α-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase. Maltogenic amylase Cyclodextrin Archaea Hyperthermophile Li, Dan aut Yin, Yongguang aut Park, Kwan-Hwa aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 85(2009), 6 vom: 26. Aug., Seite 1821-1830 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:85 year:2009 number:6 day:26 month:08 pages:1821-1830 https://doi.org/10.1007/s00253-009-2190-6 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_21 GBV_ILN_23 GBV_ILN_40 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_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 85 2009 6 26 08 1821-1830 |
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10.1007/s00253-009-2190-6 doi (DE-627)OLC2050726422 (DE-He213)s00253-009-2190-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Li, Xiaolei verfasserin aut Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. TfMA activity increased to 136% in the presence of 5 mM $ CaCl_{2} $. Maximal activity was measured toward γ-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one α-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase. Maltogenic amylase Cyclodextrin Archaea Hyperthermophile Li, Dan aut Yin, Yongguang aut Park, Kwan-Hwa aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 85(2009), 6 vom: 26. Aug., Seite 1821-1830 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:85 year:2009 number:6 day:26 month:08 pages:1821-1830 https://doi.org/10.1007/s00253-009-2190-6 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_21 GBV_ILN_23 GBV_ILN_40 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_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 85 2009 6 26 08 1821-1830 |
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English |
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Enthalten in Applied microbiology and biotechnology 85(2009), 6 vom: 26. Aug., Seite 1821-1830 volume:85 year:2009 number:6 day:26 month:08 pages:1821-1830 |
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Enthalten in Applied microbiology and biotechnology 85(2009), 6 vom: 26. Aug., Seite 1821-1830 volume:85 year:2009 number:6 day:26 month:08 pages:1821-1830 |
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Maltogenic amylase Cyclodextrin Archaea Hyperthermophile |
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Li, Xiaolei @@aut@@ Li, Dan @@aut@@ Yin, Yongguang @@aut@@ Park, Kwan-Hwa @@aut@@ |
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570 VZ 12 ssgn BIODIV DE-30 fid Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity Maltogenic amylase Cyclodextrin Archaea Hyperthermophile |
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Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity |
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characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon thermofilum pendens with extremely thermostable maltogenic amylase activity |
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Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity |
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Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. TfMA activity increased to 136% in the presence of 5 mM $ CaCl_{2} $. Maximal activity was measured toward γ-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one α-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase. © Springer-Verlag 2009 |
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Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. TfMA activity increased to 136% in the presence of 5 mM $ CaCl_{2} $. Maximal activity was measured toward γ-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one α-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase. © Springer-Verlag 2009 |
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Abstract A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. TfMA activity increased to 136% in the presence of 5 mM $ CaCl_{2} $. Maximal activity was measured toward γ-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one α-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase. © Springer-Verlag 2009 |
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Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity |
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