Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization

Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus...
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Gespeichert in:

Autor*in:	Yan Zhao [verfasserIn] Ye Yuan [verfasserIn] Xinyu Zhang [verfasserIn] Yumei Li [verfasserIn] Qiang Li [verfasserIn] Yifa Zhou [verfasserIn] Juan Gao [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2018

Schlagwörter:	pectate lyase cloning and expression ramie degumming

Übergeordnetes Werk:	In: Molecules - MDPI AG, 2003, 23(2018), 11, p 2774
Übergeordnetes Werk:	volume:23 ; year:2018 ; number:11, p 2774

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/molecules23112774

Katalog-ID:	DOAJ022689397

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520			\|a Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus polymyxa</i< KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from <i<P. polymyxa</i< KF-1 genomic DNA and expressed in <i<Escherichia coli</i<. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and <i<p</i<I of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K<sub<m</sub<, v<sub<max</sub< and k<sub<cat</sub< values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s<sup<−1</sup<, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (<i<Boehmeria nivea</i<) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing.
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700	0		\|a Juan Gao \|e verfasserin \|4 aut
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matchkey_str	article:14203049:2018----::cennoaoeplschrdlaeaiy0ettlaermpeiailsoyyak1ln
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allfields	10.3390/molecules23112774 doi (DE-627)DOAJ022689397 (DE-599)DOAJ3c92d4cd262f4de3a898195b4de1c9f4 DE-627 ger DE-627 rakwb eng QD241-441 Yan Zhao verfasserin aut Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus polymyxa</i< KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from <i<P. polymyxa</i< KF-1 genomic DNA and expressed in <i<Escherichia coli</i<. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and <i<p</i<I of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K<sub<m</sub<, v<sub<max</sub< and k<sub<cat</sub< values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s<sup<−1</sup<, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (<i<Boehmeria nivea</i<) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing. <i<Paenibacillus polymyxa</i< pectate lyase cloning and expression ramie degumming Organic chemistry Ye Yuan verfasserin aut Xinyu Zhang verfasserin aut Yumei Li verfasserin aut Qiang Li verfasserin aut Yifa Zhou verfasserin aut Juan Gao verfasserin aut In Molecules MDPI AG, 2003 23(2018), 11, p 2774 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:23 year:2018 number:11, p 2774 https://doi.org/10.3390/molecules23112774 kostenfrei https://doaj.org/article/3c92d4cd262f4de3a898195b4de1c9f4 kostenfrei https://www.mdpi.com/1420-3049/23/11/2774 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2018 11, p 2774
spelling	10.3390/molecules23112774 doi (DE-627)DOAJ022689397 (DE-599)DOAJ3c92d4cd262f4de3a898195b4de1c9f4 DE-627 ger DE-627 rakwb eng QD241-441 Yan Zhao verfasserin aut Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus polymyxa</i< KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from <i<P. polymyxa</i< KF-1 genomic DNA and expressed in <i<Escherichia coli</i<. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and <i<p</i<I of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K<sub<m</sub<, v<sub<max</sub< and k<sub<cat</sub< values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s<sup<−1</sup<, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (<i<Boehmeria nivea</i<) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing. <i<Paenibacillus polymyxa</i< pectate lyase cloning and expression ramie degumming Organic chemistry Ye Yuan verfasserin aut Xinyu Zhang verfasserin aut Yumei Li verfasserin aut Qiang Li verfasserin aut Yifa Zhou verfasserin aut Juan Gao verfasserin aut In Molecules MDPI AG, 2003 23(2018), 11, p 2774 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:23 year:2018 number:11, p 2774 https://doi.org/10.3390/molecules23112774 kostenfrei https://doaj.org/article/3c92d4cd262f4de3a898195b4de1c9f4 kostenfrei https://www.mdpi.com/1420-3049/23/11/2774 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2018 11, p 2774
allfields_unstemmed	10.3390/molecules23112774 doi (DE-627)DOAJ022689397 (DE-599)DOAJ3c92d4cd262f4de3a898195b4de1c9f4 DE-627 ger DE-627 rakwb eng QD241-441 Yan Zhao verfasserin aut Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus polymyxa</i< KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from <i<P. polymyxa</i< KF-1 genomic DNA and expressed in <i<Escherichia coli</i<. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and <i<p</i<I of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K<sub<m</sub<, v<sub<max</sub< and k<sub<cat</sub< values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s<sup<−1</sup<, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (<i<Boehmeria nivea</i<) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing. <i<Paenibacillus polymyxa</i< pectate lyase cloning and expression ramie degumming Organic chemistry Ye Yuan verfasserin aut Xinyu Zhang verfasserin aut Yumei Li verfasserin aut Qiang Li verfasserin aut Yifa Zhou verfasserin aut Juan Gao verfasserin aut In Molecules MDPI AG, 2003 23(2018), 11, p 2774 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:23 year:2018 number:11, p 2774 https://doi.org/10.3390/molecules23112774 kostenfrei https://doaj.org/article/3c92d4cd262f4de3a898195b4de1c9f4 kostenfrei https://www.mdpi.com/1420-3049/23/11/2774 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2018 11, p 2774
allfieldsGer	10.3390/molecules23112774 doi (DE-627)DOAJ022689397 (DE-599)DOAJ3c92d4cd262f4de3a898195b4de1c9f4 DE-627 ger DE-627 rakwb eng QD241-441 Yan Zhao verfasserin aut Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus polymyxa</i< KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from <i<P. polymyxa</i< KF-1 genomic DNA and expressed in <i<Escherichia coli</i<. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and <i<p</i<I of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K<sub<m</sub<, v<sub<max</sub< and k<sub<cat</sub< values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s<sup<−1</sup<, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (<i<Boehmeria nivea</i<) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing. <i<Paenibacillus polymyxa</i< pectate lyase cloning and expression ramie degumming Organic chemistry Ye Yuan verfasserin aut Xinyu Zhang verfasserin aut Yumei Li verfasserin aut Qiang Li verfasserin aut Yifa Zhou verfasserin aut Juan Gao verfasserin aut In Molecules MDPI AG, 2003 23(2018), 11, p 2774 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:23 year:2018 number:11, p 2774 https://doi.org/10.3390/molecules23112774 kostenfrei https://doaj.org/article/3c92d4cd262f4de3a898195b4de1c9f4 kostenfrei https://www.mdpi.com/1420-3049/23/11/2774 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2018 11, p 2774
allfieldsSound	10.3390/molecules23112774 doi (DE-627)DOAJ022689397 (DE-599)DOAJ3c92d4cd262f4de3a898195b4de1c9f4 DE-627 ger DE-627 rakwb eng QD241-441 Yan Zhao verfasserin aut Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus polymyxa</i< KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from <i<P. polymyxa</i< KF-1 genomic DNA and expressed in <i<Escherichia coli</i<. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and <i<p</i<I of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K<sub<m</sub<, v<sub<max</sub< and k<sub<cat</sub< values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s<sup<−1</sup<, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (<i<Boehmeria nivea</i<) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing. <i<Paenibacillus polymyxa</i< pectate lyase cloning and expression ramie degumming Organic chemistry Ye Yuan verfasserin aut Xinyu Zhang verfasserin aut Yumei Li verfasserin aut Qiang Li verfasserin aut Yifa Zhou verfasserin aut Juan Gao verfasserin aut In Molecules MDPI AG, 2003 23(2018), 11, p 2774 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:23 year:2018 number:11, p 2774 https://doi.org/10.3390/molecules23112774 kostenfrei https://doaj.org/article/3c92d4cd262f4de3a898195b4de1c9f4 kostenfrei https://www.mdpi.com/1420-3049/23/11/2774 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 23 2018 11, p 2774
language	English
source	In Molecules 23(2018), 11, p 2774 volume:23 year:2018 number:11, p 2774
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callnumber-first	Q - Science
author	Yan Zhao
spellingShingle	Yan Zhao misc QD241-441 misc <i<Paenibacillus polymyxa</i< misc pectate lyase misc cloning and expression misc ramie degumming misc Organic chemistry Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization
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topic_title	QD241-441 Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization <i<Paenibacillus polymyxa</i< pectate lyase cloning and expression ramie degumming
topic	misc QD241-441 misc <i<Paenibacillus polymyxa</i< misc pectate lyase misc cloning and expression misc ramie degumming misc Organic chemistry
topic_unstemmed	misc QD241-441 misc <i<Paenibacillus polymyxa</i< misc pectate lyase misc cloning and expression misc ramie degumming misc Organic chemistry
topic_browse	misc QD241-441 misc <i<Paenibacillus polymyxa</i< misc pectate lyase misc cloning and expression misc ramie degumming misc Organic chemistry
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title	Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization
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title_full	Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization
author_sort	Yan Zhao
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author_browse	Yan Zhao Ye Yuan Xinyu Zhang Yumei Li Qiang Li Yifa Zhou Juan Gao
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author-letter	Yan Zhao
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title_sort	screening of a novel polysaccharide lyase family 10 pectate lyase from <i<paenibacillus polymyxa</i< kf-1: cloning, expression and characterization
callnumber	QD241-441
title_auth	Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization
abstract	Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus polymyxa</i< KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from <i<P. polymyxa</i< KF-1 genomic DNA and expressed in <i<Escherichia coli</i<. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and <i<p</i<I of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K<sub<m</sub<, v<sub<max</sub< and k<sub<cat</sub< values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s<sup<−1</sup<, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (<i<Boehmeria nivea</i<) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing.
abstractGer	Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus polymyxa</i< KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from <i<P. polymyxa</i< KF-1 genomic DNA and expressed in <i<Escherichia coli</i<. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and <i<p</i<I of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K<sub<m</sub<, v<sub<max</sub< and k<sub<cat</sub< values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s<sup<−1</sup<, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (<i<Boehmeria nivea</i<) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing.
abstract_unstemmed	Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of <i<Paenibacillus polymyxa</i< KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from <i<P. polymyxa</i< KF-1 genomic DNA and expressed in <i<Escherichia coli</i<. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and <i<p</i<I of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K<sub<m</sub<, v<sub<max</sub< and k<sub<cat</sub< values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s<sup<−1</sup<, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (<i<Boehmeria nivea</i<) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing.
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title_short	Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization
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author2	Ye Yuan Xinyu Zhang Yumei Li Qiang Li Yifa Zhou Juan Gao
author2Str	Ye Yuan Xinyu Zhang Yumei Li Qiang Li Yifa Zhou Juan Gao
ppnlink	311313132
callnumber-subject	QD - Chemistry
mediatype_str_mv	c
isOA_txt	true
hochschulschrift_bool	false
doi_str	10.3390/molecules23112774
callnumber-a	QD241-441
up_date	2024-07-03T13:29:38.430Z
_version_	1803564748317392896
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Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from <i<Paenibacillus polymyxa</i< KF-1: Cloning, Expression and Characterization

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