Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis

The characterization of three laccase isoforms from Pleurotus nebrodensis is described. Isoenzymes Lac1, Lac2 and Lac3 were purified to homogeneity using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a gel filtration step on Superdex 75. The molecular weights of the...
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Autor*in:	Xianghe Yuan [verfasserIn] Guoting Tian [verfasserIn] Yongchang Zhao [verfasserIn] Liyan Zhao [verfasserIn] Hexiang Wang [verfasserIn] Tzi Bun Ng [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2016

Schlagwörter:	laccase isoenzymes enzyme characterization biochemical properties comparison Pleurotus nebrodensis

Übergeordnetes Werk:	In: Molecules - MDPI AG, 2003, 21(2016), 2, p 203
Übergeordnetes Werk:	volume:21 ; year:2016 ; number:2, p 203

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/molecules21020203

Katalog-ID:	DOAJ006382665

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520			\|a The characterization of three laccase isoforms from Pleurotus nebrodensis is described. Isoenzymes Lac1, Lac2 and Lac3 were purified to homogeneity using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a gel filtration step on Superdex 75. The molecular weights of the purified laccases were estimated to be 68, 64 and 51 kDa, respectively. The isoenzymes demonstrated the same optimum pH at 3.0 but slightly different temperature optima: 50–60 °C for Lac1 and Lac3 and 60 °C for Lac2. Lac2 was always more stable than the other two isoforms and exposure to 50 °C for 120 min caused 30% loss in activity. Lac2 was relatively less stable than the other two isoforms when exposed to the pH range of 3.0–8.0 for 24 h, but inactivation only occurred initially, with around 70% residual activity being maintained during the whole process. Oxidative ability towards aromatic compounds varied substantially among the isoforms and each of them displayed preference toward some substrates. Kinetic constants (Km, Kcat) were determined by using a 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) assay, with Lac3 showing the best affinity and Lac2 displaying the highest catalytic efficiency. Amino acid sequences from peptides derived from digestion of isoenzymes showed great consistency with laccases in the databases.
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allfields	10.3390/molecules21020203 doi (DE-627)DOAJ006382665 (DE-599)DOAJ9b31b3db89be4764beedd97dbddb3eeb DE-627 ger DE-627 rakwb eng QD241-441 Xianghe Yuan verfasserin aut Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The characterization of three laccase isoforms from Pleurotus nebrodensis is described. Isoenzymes Lac1, Lac2 and Lac3 were purified to homogeneity using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a gel filtration step on Superdex 75. The molecular weights of the purified laccases were estimated to be 68, 64 and 51 kDa, respectively. The isoenzymes demonstrated the same optimum pH at 3.0 but slightly different temperature optima: 50–60 °C for Lac1 and Lac3 and 60 °C for Lac2. Lac2 was always more stable than the other two isoforms and exposure to 50 °C for 120 min caused 30% loss in activity. Lac2 was relatively less stable than the other two isoforms when exposed to the pH range of 3.0–8.0 for 24 h, but inactivation only occurred initially, with around 70% residual activity being maintained during the whole process. Oxidative ability towards aromatic compounds varied substantially among the isoforms and each of them displayed preference toward some substrates. Kinetic constants (Km, Kcat) were determined by using a 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) assay, with Lac3 showing the best affinity and Lac2 displaying the highest catalytic efficiency. Amino acid sequences from peptides derived from digestion of isoenzymes showed great consistency with laccases in the databases. laccase isoenzymes enzyme characterization biochemical properties comparison Pleurotus nebrodensis Organic chemistry Guoting Tian verfasserin aut Yongchang Zhao verfasserin aut Liyan Zhao verfasserin aut Hexiang Wang verfasserin aut Tzi Bun Ng verfasserin aut In Molecules MDPI AG, 2003 21(2016), 2, p 203 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:21 year:2016 number:2, p 203 https://doi.org/10.3390/molecules21020203 kostenfrei https://doaj.org/article/9b31b3db89be4764beedd97dbddb3eeb kostenfrei http://www.mdpi.com/1420-3049/21/2/203 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ 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 21 2016 2, p 203
spelling	10.3390/molecules21020203 doi (DE-627)DOAJ006382665 (DE-599)DOAJ9b31b3db89be4764beedd97dbddb3eeb DE-627 ger DE-627 rakwb eng QD241-441 Xianghe Yuan verfasserin aut Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The characterization of three laccase isoforms from Pleurotus nebrodensis is described. Isoenzymes Lac1, Lac2 and Lac3 were purified to homogeneity using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a gel filtration step on Superdex 75. The molecular weights of the purified laccases were estimated to be 68, 64 and 51 kDa, respectively. The isoenzymes demonstrated the same optimum pH at 3.0 but slightly different temperature optima: 50–60 °C for Lac1 and Lac3 and 60 °C for Lac2. Lac2 was always more stable than the other two isoforms and exposure to 50 °C for 120 min caused 30% loss in activity. Lac2 was relatively less stable than the other two isoforms when exposed to the pH range of 3.0–8.0 for 24 h, but inactivation only occurred initially, with around 70% residual activity being maintained during the whole process. Oxidative ability towards aromatic compounds varied substantially among the isoforms and each of them displayed preference toward some substrates. Kinetic constants (Km, Kcat) were determined by using a 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) assay, with Lac3 showing the best affinity and Lac2 displaying the highest catalytic efficiency. Amino acid sequences from peptides derived from digestion of isoenzymes showed great consistency with laccases in the databases. laccase isoenzymes enzyme characterization biochemical properties comparison Pleurotus nebrodensis Organic chemistry Guoting Tian verfasserin aut Yongchang Zhao verfasserin aut Liyan Zhao verfasserin aut Hexiang Wang verfasserin aut Tzi Bun Ng verfasserin aut In Molecules MDPI AG, 2003 21(2016), 2, p 203 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:21 year:2016 number:2, p 203 https://doi.org/10.3390/molecules21020203 kostenfrei https://doaj.org/article/9b31b3db89be4764beedd97dbddb3eeb kostenfrei http://www.mdpi.com/1420-3049/21/2/203 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ 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 21 2016 2, p 203
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allfieldsSound	10.3390/molecules21020203 doi (DE-627)DOAJ006382665 (DE-599)DOAJ9b31b3db89be4764beedd97dbddb3eeb DE-627 ger DE-627 rakwb eng QD241-441 Xianghe Yuan verfasserin aut Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The characterization of three laccase isoforms from Pleurotus nebrodensis is described. Isoenzymes Lac1, Lac2 and Lac3 were purified to homogeneity using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a gel filtration step on Superdex 75. The molecular weights of the purified laccases were estimated to be 68, 64 and 51 kDa, respectively. The isoenzymes demonstrated the same optimum pH at 3.0 but slightly different temperature optima: 50–60 °C for Lac1 and Lac3 and 60 °C for Lac2. Lac2 was always more stable than the other two isoforms and exposure to 50 °C for 120 min caused 30% loss in activity. Lac2 was relatively less stable than the other two isoforms when exposed to the pH range of 3.0–8.0 for 24 h, but inactivation only occurred initially, with around 70% residual activity being maintained during the whole process. Oxidative ability towards aromatic compounds varied substantially among the isoforms and each of them displayed preference toward some substrates. Kinetic constants (Km, Kcat) were determined by using a 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) assay, with Lac3 showing the best affinity and Lac2 displaying the highest catalytic efficiency. Amino acid sequences from peptides derived from digestion of isoenzymes showed great consistency with laccases in the databases. laccase isoenzymes enzyme characterization biochemical properties comparison Pleurotus nebrodensis Organic chemistry Guoting Tian verfasserin aut Yongchang Zhao verfasserin aut Liyan Zhao verfasserin aut Hexiang Wang verfasserin aut Tzi Bun Ng verfasserin aut In Molecules MDPI AG, 2003 21(2016), 2, p 203 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:21 year:2016 number:2, p 203 https://doi.org/10.3390/molecules21020203 kostenfrei https://doaj.org/article/9b31b3db89be4764beedd97dbddb3eeb kostenfrei http://www.mdpi.com/1420-3049/21/2/203 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ 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 21 2016 2, p 203
language	English
source	In Molecules 21(2016), 2, p 203 volume:21 year:2016 number:2, p 203
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topic_facet	laccase isoenzymes enzyme characterization biochemical properties comparison Pleurotus nebrodensis Organic chemistry
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authorswithroles_txt_mv	Xianghe Yuan @@aut@@ Guoting Tian @@aut@@ Yongchang Zhao @@aut@@ Liyan Zhao @@aut@@ Hexiang Wang @@aut@@ Tzi Bun Ng @@aut@@
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callnumber-first	Q - Science
author	Xianghe Yuan
spellingShingle	Xianghe Yuan misc QD241-441 misc laccase isoenzymes misc enzyme characterization misc biochemical properties comparison misc Pleurotus nebrodensis misc Organic chemistry Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis
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topic_title	QD241-441 Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis laccase isoenzymes enzyme characterization biochemical properties comparison Pleurotus nebrodensis
topic	misc QD241-441 misc laccase isoenzymes misc enzyme characterization misc biochemical properties comparison misc Pleurotus nebrodensis misc Organic chemistry
topic_unstemmed	misc QD241-441 misc laccase isoenzymes misc enzyme characterization misc biochemical properties comparison misc Pleurotus nebrodensis misc Organic chemistry
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title	Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis
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title_full	Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis
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title_sort	biochemical characteristics of three laccase isoforms from the basidiomycete pleurotus nebrodensis
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title_auth	Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis
abstract	The characterization of three laccase isoforms from Pleurotus nebrodensis is described. Isoenzymes Lac1, Lac2 and Lac3 were purified to homogeneity using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a gel filtration step on Superdex 75. The molecular weights of the purified laccases were estimated to be 68, 64 and 51 kDa, respectively. The isoenzymes demonstrated the same optimum pH at 3.0 but slightly different temperature optima: 50–60 °C for Lac1 and Lac3 and 60 °C for Lac2. Lac2 was always more stable than the other two isoforms and exposure to 50 °C for 120 min caused 30% loss in activity. Lac2 was relatively less stable than the other two isoforms when exposed to the pH range of 3.0–8.0 for 24 h, but inactivation only occurred initially, with around 70% residual activity being maintained during the whole process. Oxidative ability towards aromatic compounds varied substantially among the isoforms and each of them displayed preference toward some substrates. Kinetic constants (Km, Kcat) were determined by using a 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) assay, with Lac3 showing the best affinity and Lac2 displaying the highest catalytic efficiency. Amino acid sequences from peptides derived from digestion of isoenzymes showed great consistency with laccases in the databases.
abstractGer	The characterization of three laccase isoforms from Pleurotus nebrodensis is described. Isoenzymes Lac1, Lac2 and Lac3 were purified to homogeneity using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a gel filtration step on Superdex 75. The molecular weights of the purified laccases were estimated to be 68, 64 and 51 kDa, respectively. The isoenzymes demonstrated the same optimum pH at 3.0 but slightly different temperature optima: 50–60 °C for Lac1 and Lac3 and 60 °C for Lac2. Lac2 was always more stable than the other two isoforms and exposure to 50 °C for 120 min caused 30% loss in activity. Lac2 was relatively less stable than the other two isoforms when exposed to the pH range of 3.0–8.0 for 24 h, but inactivation only occurred initially, with around 70% residual activity being maintained during the whole process. Oxidative ability towards aromatic compounds varied substantially among the isoforms and each of them displayed preference toward some substrates. Kinetic constants (Km, Kcat) were determined by using a 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) assay, with Lac3 showing the best affinity and Lac2 displaying the highest catalytic efficiency. Amino acid sequences from peptides derived from digestion of isoenzymes showed great consistency with laccases in the databases.
abstract_unstemmed	The characterization of three laccase isoforms from Pleurotus nebrodensis is described. Isoenzymes Lac1, Lac2 and Lac3 were purified to homogeneity using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a gel filtration step on Superdex 75. The molecular weights of the purified laccases were estimated to be 68, 64 and 51 kDa, respectively. The isoenzymes demonstrated the same optimum pH at 3.0 but slightly different temperature optima: 50–60 °C for Lac1 and Lac3 and 60 °C for Lac2. Lac2 was always more stable than the other two isoforms and exposure to 50 °C for 120 min caused 30% loss in activity. Lac2 was relatively less stable than the other two isoforms when exposed to the pH range of 3.0–8.0 for 24 h, but inactivation only occurred initially, with around 70% residual activity being maintained during the whole process. Oxidative ability towards aromatic compounds varied substantially among the isoforms and each of them displayed preference toward some substrates. Kinetic constants (Km, Kcat) were determined by using a 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) assay, with Lac3 showing the best affinity and Lac2 displaying the highest catalytic efficiency. Amino acid sequences from peptides derived from digestion of isoenzymes showed great consistency with laccases in the databases.
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title_short	Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis
url	https://doi.org/10.3390/molecules21020203 https://doaj.org/article/9b31b3db89be4764beedd97dbddb3eeb http://www.mdpi.com/1420-3049/21/2/203 https://doaj.org/toc/1420-3049
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up_date	2024-07-03T20:36:24.587Z
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Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis

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