A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics
Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the pres...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Sasaki, Masato [verfasserIn] Koide, Osamu [verfasserIn] Kobayashi, Tohru [verfasserIn] Usami, Ron [verfasserIn] Horikoshi, Koki [verfasserIn] |
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Englisch |
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2014 |
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Enthalten in: Extremophiles - Springer-Verlag, 2001, 19(2014), 1 vom: 11. Sept., Seite 119-125 |
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volume:19 ; year:2014 ; number:1 ; day:11 ; month:09 ; pages:119-125 |
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10.1007/s00792-014-0691-4 |
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| 520 | |a Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin. | ||
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10.1007/s00792-014-0691-4 doi (DE-627)SPR007863152 (SPR)s00792-014-0691-4-e DE-627 ger DE-627 rakwb eng Sasaki, Masato verfasserin aut A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin. Pectate lyase (dpeaa)DE-He213 Subseafloor (dpeaa)DE-He213 Chikyu (dpeaa)DE-He213 Suruga Bay (dpeaa)DE-He213 Koide, Osamu verfasserin aut Kobayashi, Tohru verfasserin aut Usami, Ron verfasserin aut Horikoshi, Koki verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 19(2014), 1 vom: 11. Sept., Seite 119-125 (DE-627)SPR007852657 nnns volume:19 year:2014 number:1 day:11 month:09 pages:119-125 https://dx.doi.org/10.1007/s00792-014-0691-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 19 2014 1 11 09 119-125 |
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10.1007/s00792-014-0691-4 doi (DE-627)SPR007863152 (SPR)s00792-014-0691-4-e DE-627 ger DE-627 rakwb eng Sasaki, Masato verfasserin aut A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin. Pectate lyase (dpeaa)DE-He213 Subseafloor (dpeaa)DE-He213 Chikyu (dpeaa)DE-He213 Suruga Bay (dpeaa)DE-He213 Koide, Osamu verfasserin aut Kobayashi, Tohru verfasserin aut Usami, Ron verfasserin aut Horikoshi, Koki verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 19(2014), 1 vom: 11. Sept., Seite 119-125 (DE-627)SPR007852657 nnns volume:19 year:2014 number:1 day:11 month:09 pages:119-125 https://dx.doi.org/10.1007/s00792-014-0691-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 19 2014 1 11 09 119-125 |
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10.1007/s00792-014-0691-4 doi (DE-627)SPR007863152 (SPR)s00792-014-0691-4-e DE-627 ger DE-627 rakwb eng Sasaki, Masato verfasserin aut A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin. Pectate lyase (dpeaa)DE-He213 Subseafloor (dpeaa)DE-He213 Chikyu (dpeaa)DE-He213 Suruga Bay (dpeaa)DE-He213 Koide, Osamu verfasserin aut Kobayashi, Tohru verfasserin aut Usami, Ron verfasserin aut Horikoshi, Koki verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 19(2014), 1 vom: 11. Sept., Seite 119-125 (DE-627)SPR007852657 nnns volume:19 year:2014 number:1 day:11 month:09 pages:119-125 https://dx.doi.org/10.1007/s00792-014-0691-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 19 2014 1 11 09 119-125 |
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10.1007/s00792-014-0691-4 doi (DE-627)SPR007863152 (SPR)s00792-014-0691-4-e DE-627 ger DE-627 rakwb eng Sasaki, Masato verfasserin aut A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin. Pectate lyase (dpeaa)DE-He213 Subseafloor (dpeaa)DE-He213 Chikyu (dpeaa)DE-He213 Suruga Bay (dpeaa)DE-He213 Koide, Osamu verfasserin aut Kobayashi, Tohru verfasserin aut Usami, Ron verfasserin aut Horikoshi, Koki verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 19(2014), 1 vom: 11. Sept., Seite 119-125 (DE-627)SPR007852657 nnns volume:19 year:2014 number:1 day:11 month:09 pages:119-125 https://dx.doi.org/10.1007/s00792-014-0691-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 19 2014 1 11 09 119-125 |
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10.1007/s00792-014-0691-4 doi (DE-627)SPR007863152 (SPR)s00792-014-0691-4-e DE-627 ger DE-627 rakwb eng Sasaki, Masato verfasserin aut A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin. Pectate lyase (dpeaa)DE-He213 Subseafloor (dpeaa)DE-He213 Chikyu (dpeaa)DE-He213 Suruga Bay (dpeaa)DE-He213 Koide, Osamu verfasserin aut Kobayashi, Tohru verfasserin aut Usami, Ron verfasserin aut Horikoshi, Koki verfasserin aut Enthalten in Extremophiles Springer-Verlag, 2001 19(2014), 1 vom: 11. Sept., Seite 119-125 (DE-627)SPR007852657 nnns volume:19 year:2014 number:1 day:11 month:09 pages:119-125 https://dx.doi.org/10.1007/s00792-014-0691-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 19 2014 1 11 09 119-125 |
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A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics |
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Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin. |
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Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin. |
| abstract_unstemmed |
Abstract A novel pectate lyase of a deep subseafloor bacterium, Georgenia muralis strain JAM 3H7-3 (JCM19733), was purified to homogeneity from a culture broth by an anion exchange chromatography, followed by heat treatment of the enzyme solution at 60 °C for 30 min, and a gel filtration in the presence of SDS. The purified enzyme (Pel-S2) had a molecular mass of ~51 kDa by SDS-PAGE and ~75 kDa by gel filtration. In contrast, without heat treatment, the purified enzyme in SDS sample buffer was found to consist of 23- and 23.5-kDa polypeptides by SDS-PAGE. The enzyme was gradually inactivated by heat treatment with and without SDS in parallel with a shift of polypeptides molecular masses from 23 and 23.5 to 51 kDa on SDS-PAGE. Pel-S2 degraded pectate optimally at pH 10 in a glycine buffer and temperature of 50 °C. The enzyme showed relatively broad substrate specificity toward pectic acid and pectin. |
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| title_short |
A pectate lyase from a deep subseafloor Georgenia muralis with unusual molecular characteristics |
| url |
https://dx.doi.org/10.1007/s00792-014-0691-4 |
| remote_bool |
true |
| author2 |
Koide, Osamu Kobayashi, Tohru Usami, Ron Horikoshi, Koki |
| author2Str |
Koide, Osamu Kobayashi, Tohru Usami, Ron Horikoshi, Koki |
| ppnlink |
SPR007852657 |
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c |
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false |
| hochschulschrift_bool |
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| doi_str |
10.1007/s00792-014-0691-4 |
| up_date |
2024-07-03T15:43:58.311Z |
| _version_ |
1803573199700492288 |
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