Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase

Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The matu...
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Gespeichert in:

Autor*in:	Berensmeier, S. [verfasserIn] Singh, S. A. Meens, J. Buchholz, K.

Format:	Artikel
Sprache:	Englisch

Erschienen:	2003

Schlagwörter:	Pectin Sugar Beet Lyase Bacillus Licheniformis Pectate Lyase

Anmerkung:	© Springer-Verlag 2003

Übergeordnetes Werk:	Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 64(2003), 4 vom: 13. Dez., Seite 560-567
Übergeordnetes Werk:	volume:64 ; year:2003 ; number:4 ; day:13 ; month:12 ; pages:560-567

Links:	Volltext

DOI / URN:	10.1007/s00253-003-1446-9

Katalog-ID:	OLC205069945X

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520			\|a Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The mature PelA showed significant homology to other pectate lyases belonging to polysaccharide lyase family 1, such as enzymes from different Bacillus spp. and Erwinia chrysanthemi. The pelA gene was expressed in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag, allowing purification to near homogeneity in a one-step procedure. The values for the kinetic parameters Km and Vmax of the fusion protein were 0.56 g/l and 51 µmol/min, respectively. The activity of purified $ PelA^{His} $ was inhibited in the presence of excess substrate. Characterization of product formation revealed unsaturated trigalacturonate as the main product. The yields of unsaturated trigalacturonic acids were further examined for the substrates polygalacturonic acid, citrus pectin and sugar-beet pectin.
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allfields	10.1007/s00253-003-1446-9 doi (DE-627)OLC205069945X (DE-He213)s00253-003-1446-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Berensmeier, S. verfasserin aut Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase 2003 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The mature PelA showed significant homology to other pectate lyases belonging to polysaccharide lyase family 1, such as enzymes from different Bacillus spp. and Erwinia chrysanthemi. The pelA gene was expressed in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag, allowing purification to near homogeneity in a one-step procedure. The values for the kinetic parameters Km and Vmax of the fusion protein were 0.56 g/l and 51 µmol/min, respectively. The activity of purified $ PelA^{His} $ was inhibited in the presence of excess substrate. Characterization of product formation revealed unsaturated trigalacturonate as the main product. The yields of unsaturated trigalacturonic acids were further examined for the substrates polygalacturonic acid, citrus pectin and sugar-beet pectin. Pectin Sugar Beet Lyase Bacillus Licheniformis Pectate Lyase Singh, S. A. aut Meens, J. aut Buchholz, K. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 64(2003), 4 vom: 13. Dez., Seite 560-567 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:64 year:2003 number:4 day:13 month:12 pages:560-567 https://doi.org/10.1007/s00253-003-1446-9 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_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 64 2003 4 13 12 560-567
spelling	10.1007/s00253-003-1446-9 doi (DE-627)OLC205069945X (DE-He213)s00253-003-1446-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Berensmeier, S. verfasserin aut Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase 2003 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The mature PelA showed significant homology to other pectate lyases belonging to polysaccharide lyase family 1, such as enzymes from different Bacillus spp. and Erwinia chrysanthemi. The pelA gene was expressed in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag, allowing purification to near homogeneity in a one-step procedure. The values for the kinetic parameters Km and Vmax of the fusion protein were 0.56 g/l and 51 µmol/min, respectively. The activity of purified $ PelA^{His} $ was inhibited in the presence of excess substrate. Characterization of product formation revealed unsaturated trigalacturonate as the main product. The yields of unsaturated trigalacturonic acids were further examined for the substrates polygalacturonic acid, citrus pectin and sugar-beet pectin. Pectin Sugar Beet Lyase Bacillus Licheniformis Pectate Lyase Singh, S. A. aut Meens, J. aut Buchholz, K. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 64(2003), 4 vom: 13. Dez., Seite 560-567 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:64 year:2003 number:4 day:13 month:12 pages:560-567 https://doi.org/10.1007/s00253-003-1446-9 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_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 64 2003 4 13 12 560-567
allfields_unstemmed	10.1007/s00253-003-1446-9 doi (DE-627)OLC205069945X (DE-He213)s00253-003-1446-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Berensmeier, S. verfasserin aut Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase 2003 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The mature PelA showed significant homology to other pectate lyases belonging to polysaccharide lyase family 1, such as enzymes from different Bacillus spp. and Erwinia chrysanthemi. The pelA gene was expressed in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag, allowing purification to near homogeneity in a one-step procedure. The values for the kinetic parameters Km and Vmax of the fusion protein were 0.56 g/l and 51 µmol/min, respectively. The activity of purified $ PelA^{His} $ was inhibited in the presence of excess substrate. Characterization of product formation revealed unsaturated trigalacturonate as the main product. The yields of unsaturated trigalacturonic acids were further examined for the substrates polygalacturonic acid, citrus pectin and sugar-beet pectin. Pectin Sugar Beet Lyase Bacillus Licheniformis Pectate Lyase Singh, S. A. aut Meens, J. aut Buchholz, K. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 64(2003), 4 vom: 13. Dez., Seite 560-567 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:64 year:2003 number:4 day:13 month:12 pages:560-567 https://doi.org/10.1007/s00253-003-1446-9 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_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 64 2003 4 13 12 560-567
allfieldsGer	10.1007/s00253-003-1446-9 doi (DE-627)OLC205069945X (DE-He213)s00253-003-1446-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Berensmeier, S. verfasserin aut Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase 2003 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The mature PelA showed significant homology to other pectate lyases belonging to polysaccharide lyase family 1, such as enzymes from different Bacillus spp. and Erwinia chrysanthemi. The pelA gene was expressed in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag, allowing purification to near homogeneity in a one-step procedure. The values for the kinetic parameters Km and Vmax of the fusion protein were 0.56 g/l and 51 µmol/min, respectively. The activity of purified $ PelA^{His} $ was inhibited in the presence of excess substrate. Characterization of product formation revealed unsaturated trigalacturonate as the main product. The yields of unsaturated trigalacturonic acids were further examined for the substrates polygalacturonic acid, citrus pectin and sugar-beet pectin. Pectin Sugar Beet Lyase Bacillus Licheniformis Pectate Lyase Singh, S. A. aut Meens, J. aut Buchholz, K. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 64(2003), 4 vom: 13. Dez., Seite 560-567 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:64 year:2003 number:4 day:13 month:12 pages:560-567 https://doi.org/10.1007/s00253-003-1446-9 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_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 64 2003 4 13 12 560-567
allfieldsSound	10.1007/s00253-003-1446-9 doi (DE-627)OLC205069945X (DE-He213)s00253-003-1446-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Berensmeier, S. verfasserin aut Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase 2003 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2003 Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The mature PelA showed significant homology to other pectate lyases belonging to polysaccharide lyase family 1, such as enzymes from different Bacillus spp. and Erwinia chrysanthemi. The pelA gene was expressed in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag, allowing purification to near homogeneity in a one-step procedure. The values for the kinetic parameters Km and Vmax of the fusion protein were 0.56 g/l and 51 µmol/min, respectively. The activity of purified $ PelA^{His} $ was inhibited in the presence of excess substrate. Characterization of product formation revealed unsaturated trigalacturonate as the main product. The yields of unsaturated trigalacturonic acids were further examined for the substrates polygalacturonic acid, citrus pectin and sugar-beet pectin. Pectin Sugar Beet Lyase Bacillus Licheniformis Pectate Lyase Singh, S. A. aut Meens, J. aut Buchholz, K. aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 64(2003), 4 vom: 13. Dez., Seite 560-567 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:64 year:2003 number:4 day:13 month:12 pages:560-567 https://doi.org/10.1007/s00253-003-1446-9 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_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_252 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4307 GBV_ILN_4310 AR 64 2003 4 13 12 560-567
language	English
source	Enthalten in Applied microbiology and biotechnology 64(2003), 4 vom: 13. Dez., Seite 560-567 volume:64 year:2003 number:4 day:13 month:12 pages:560-567
sourceStr	Enthalten in Applied microbiology and biotechnology 64(2003), 4 vom: 13. Dez., Seite 560-567 volume:64 year:2003 number:4 day:13 month:12 pages:560-567
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Pectin Sugar Beet Lyase Bacillus Licheniformis Pectate Lyase
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container_title	Applied microbiology and biotechnology
authorswithroles_txt_mv	Berensmeier, S. @@aut@@ Singh, S. A. @@aut@@ Meens, J. @@aut@@ Buchholz, K. @@aut@@
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author	Berensmeier, S.
spellingShingle	Berensmeier, S. ddc 570 ssgn 12 fid BIODIV misc Pectin misc Sugar Beet misc Lyase misc Bacillus Licheniformis misc Pectate Lyase Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase
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topic_title	570 VZ 12 ssgn BIODIV DE-30 fid Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase Pectin Sugar Beet Lyase Bacillus Licheniformis Pectate Lyase
topic	ddc 570 ssgn 12 fid BIODIV misc Pectin misc Sugar Beet misc Lyase misc Bacillus Licheniformis misc Pectate Lyase
topic_unstemmed	ddc 570 ssgn 12 fid BIODIV misc Pectin misc Sugar Beet misc Lyase misc Bacillus Licheniformis misc Pectate Lyase
topic_browse	ddc 570 ssgn 12 fid BIODIV misc Pectin misc Sugar Beet misc Lyase misc Bacillus Licheniformis misc Pectate Lyase
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title	Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase
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title_full	Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase
author_sort	Berensmeier, S.
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author_browse	Berensmeier, S. Singh, S. A. Meens, J. Buchholz, K.
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title_sort	cloning of the pela gene from bacillus licheniformis 14a and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase
title_auth	Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase
abstract	Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The mature PelA showed significant homology to other pectate lyases belonging to polysaccharide lyase family 1, such as enzymes from different Bacillus spp. and Erwinia chrysanthemi. The pelA gene was expressed in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag, allowing purification to near homogeneity in a one-step procedure. The values for the kinetic parameters Km and Vmax of the fusion protein were 0.56 g/l and 51 µmol/min, respectively. The activity of purified $ PelA^{His} $ was inhibited in the presence of excess substrate. Characterization of product formation revealed unsaturated trigalacturonate as the main product. The yields of unsaturated trigalacturonic acids were further examined for the substrates polygalacturonic acid, citrus pectin and sugar-beet pectin. © Springer-Verlag 2003
abstractGer	Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The mature PelA showed significant homology to other pectate lyases belonging to polysaccharide lyase family 1, such as enzymes from different Bacillus spp. and Erwinia chrysanthemi. The pelA gene was expressed in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag, allowing purification to near homogeneity in a one-step procedure. The values for the kinetic parameters Km and Vmax of the fusion protein were 0.56 g/l and 51 µmol/min, respectively. The activity of purified $ PelA^{His} $ was inhibited in the presence of excess substrate. Characterization of product formation revealed unsaturated trigalacturonate as the main product. The yields of unsaturated trigalacturonic acids were further examined for the substrates polygalacturonic acid, citrus pectin and sugar-beet pectin. © Springer-Verlag 2003
abstract_unstemmed	Abstract The pectate lyase gene pelA from alkaliphilic Bacillus licheniformis strain 14A was cloned and sequenced. The nucleotide sequence corresponded to an open reading frame of 1,026 bp that codes for a 39 amino acid signal peptide and a mature protein with a molecular mass of 33,451 Da. The mature PelA showed significant homology to other pectate lyases belonging to polysaccharide lyase family 1, such as enzymes from different Bacillus spp. and Erwinia chrysanthemi. The pelA gene was expressed in Escherichia coli as a recombinant fusion protein containing a C-terminal His-tag, allowing purification to near homogeneity in a one-step procedure. The values for the kinetic parameters Km and Vmax of the fusion protein were 0.56 g/l and 51 µmol/min, respectively. The activity of purified $ PelA^{His} $ was inhibited in the presence of excess substrate. Characterization of product formation revealed unsaturated trigalacturonate as the main product. The yields of unsaturated trigalacturonic acids were further examined for the substrates polygalacturonic acid, citrus pectin and sugar-beet pectin. © Springer-Verlag 2003
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title_short	Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase
url	https://doi.org/10.1007/s00253-003-1446-9
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