Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus
Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of co...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Justo, Priscila Innocenti [verfasserIn] Corrêa, Juliana Moço [verfasserIn] Maller, Alexandre [verfasserIn] Kadowaki, Marina Kimiko [verfasserIn] da Conceição-Silva, José Luis [verfasserIn] Gandra, Rinaldo Ferreira [verfasserIn] Simão, Rita de Cássia Garcia [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Antonie van Leeuwenhoek - Dordrecht [u.a.] : Springer Science + Business Media B.V, 1934, 108(2015), 4 vom: 12. Aug., Seite 993-1007 |
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| Übergeordnetes Werk: |
volume:108 ; year:2015 ; number:4 ; day:12 ; month:08 ; pages:993-1007 |
| Links: |
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| DOI / URN: |
10.1007/s10482-015-0552-x |
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| Katalog-ID: |
SPR01037891X |
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| 100 | 1 | |a Justo, Priscila Innocenti |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus |
| 264 | 1 | |c 2015 | |
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| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 520 | |a Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). To date, this is the first report to demonstrate the characterization of a GH3-BglX family member in C. crescentus that may have applications in biotechnological processes (i.e., the simultaneous saccharification process) because the multifunctional enzyme could play an important role in bacterial hemicellulose degradation. | ||
| 650 | 4 | |a Cloning and expression |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a genes |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Hemicellulose |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Agro-industrial residues |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Corrêa, Juliana Moço |e verfasserin |4 aut | |
| 700 | 1 | |a Maller, Alexandre |e verfasserin |4 aut | |
| 700 | 1 | |a Kadowaki, Marina Kimiko |e verfasserin |4 aut | |
| 700 | 1 | |a da Conceição-Silva, José Luis |e verfasserin |4 aut | |
| 700 | 1 | |a Gandra, Rinaldo Ferreira |e verfasserin |4 aut | |
| 700 | 1 | |a Simão, Rita de Cássia Garcia |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Antonie van Leeuwenhoek |d Dordrecht [u.a.] : Springer Science + Business Media B.V, 1934 |g 108(2015), 4 vom: 12. Aug., Seite 993-1007 |w (DE-627)270929355 |w (DE-600)1478112-8 |x 1572-9699 |7 nnns |
| 773 | 1 | 8 | |g volume:108 |g year:2015 |g number:4 |g day:12 |g month:08 |g pages:993-1007 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s10482-015-0552-x |z lizenzpflichtig |3 Volltext |
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| 912 | |a GBV_ILN_2065 | ||
| 912 | |a GBV_ILN_2068 | ||
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| 912 | |a GBV_ILN_2086 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2107 | ||
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| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2119 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
| 912 | |a GBV_ILN_2143 | ||
| 912 | |a GBV_ILN_2144 | ||
| 912 | |a GBV_ILN_2147 | ||
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10.1007/s10482-015-0552-x doi (DE-627)SPR01037891X (SPR)s10482-015-0552-x-e DE-627 ger DE-627 rakwb eng 570 610 ASE 42.30 bkl Justo, Priscila Innocenti verfasserin aut Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). To date, this is the first report to demonstrate the characterization of a GH3-BglX family member in C. crescentus that may have applications in biotechnological processes (i.e., the simultaneous saccharification process) because the multifunctional enzyme could play an important role in bacterial hemicellulose degradation. Cloning and expression (dpeaa)DE-He213 genes (dpeaa)DE-He213 Hemicellulose (dpeaa)DE-He213 Agro-industrial residues (dpeaa)DE-He213 Corrêa, Juliana Moço verfasserin aut Maller, Alexandre verfasserin aut Kadowaki, Marina Kimiko verfasserin aut da Conceição-Silva, José Luis verfasserin aut Gandra, Rinaldo Ferreira verfasserin aut Simão, Rita de Cássia Garcia verfasserin aut Enthalten in Antonie van Leeuwenhoek Dordrecht [u.a.] : Springer Science + Business Media B.V, 1934 108(2015), 4 vom: 12. Aug., Seite 993-1007 (DE-627)270929355 (DE-600)1478112-8 1572-9699 nnns volume:108 year:2015 number:4 day:12 month:08 pages:993-1007 https://dx.doi.org/10.1007/s10482-015-0552-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.30 ASE AR 108 2015 4 12 08 993-1007 |
| spelling |
10.1007/s10482-015-0552-x doi (DE-627)SPR01037891X (SPR)s10482-015-0552-x-e DE-627 ger DE-627 rakwb eng 570 610 ASE 42.30 bkl Justo, Priscila Innocenti verfasserin aut Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). To date, this is the first report to demonstrate the characterization of a GH3-BglX family member in C. crescentus that may have applications in biotechnological processes (i.e., the simultaneous saccharification process) because the multifunctional enzyme could play an important role in bacterial hemicellulose degradation. Cloning and expression (dpeaa)DE-He213 genes (dpeaa)DE-He213 Hemicellulose (dpeaa)DE-He213 Agro-industrial residues (dpeaa)DE-He213 Corrêa, Juliana Moço verfasserin aut Maller, Alexandre verfasserin aut Kadowaki, Marina Kimiko verfasserin aut da Conceição-Silva, José Luis verfasserin aut Gandra, Rinaldo Ferreira verfasserin aut Simão, Rita de Cássia Garcia verfasserin aut Enthalten in Antonie van Leeuwenhoek Dordrecht [u.a.] : Springer Science + Business Media B.V, 1934 108(2015), 4 vom: 12. Aug., Seite 993-1007 (DE-627)270929355 (DE-600)1478112-8 1572-9699 nnns volume:108 year:2015 number:4 day:12 month:08 pages:993-1007 https://dx.doi.org/10.1007/s10482-015-0552-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.30 ASE AR 108 2015 4 12 08 993-1007 |
| allfields_unstemmed |
10.1007/s10482-015-0552-x doi (DE-627)SPR01037891X (SPR)s10482-015-0552-x-e DE-627 ger DE-627 rakwb eng 570 610 ASE 42.30 bkl Justo, Priscila Innocenti verfasserin aut Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). To date, this is the first report to demonstrate the characterization of a GH3-BglX family member in C. crescentus that may have applications in biotechnological processes (i.e., the simultaneous saccharification process) because the multifunctional enzyme could play an important role in bacterial hemicellulose degradation. Cloning and expression (dpeaa)DE-He213 genes (dpeaa)DE-He213 Hemicellulose (dpeaa)DE-He213 Agro-industrial residues (dpeaa)DE-He213 Corrêa, Juliana Moço verfasserin aut Maller, Alexandre verfasserin aut Kadowaki, Marina Kimiko verfasserin aut da Conceição-Silva, José Luis verfasserin aut Gandra, Rinaldo Ferreira verfasserin aut Simão, Rita de Cássia Garcia verfasserin aut Enthalten in Antonie van Leeuwenhoek Dordrecht [u.a.] : Springer Science + Business Media B.V, 1934 108(2015), 4 vom: 12. Aug., Seite 993-1007 (DE-627)270929355 (DE-600)1478112-8 1572-9699 nnns volume:108 year:2015 number:4 day:12 month:08 pages:993-1007 https://dx.doi.org/10.1007/s10482-015-0552-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.30 ASE AR 108 2015 4 12 08 993-1007 |
| allfieldsGer |
10.1007/s10482-015-0552-x doi (DE-627)SPR01037891X (SPR)s10482-015-0552-x-e DE-627 ger DE-627 rakwb eng 570 610 ASE 42.30 bkl Justo, Priscila Innocenti verfasserin aut Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). To date, this is the first report to demonstrate the characterization of a GH3-BglX family member in C. crescentus that may have applications in biotechnological processes (i.e., the simultaneous saccharification process) because the multifunctional enzyme could play an important role in bacterial hemicellulose degradation. Cloning and expression (dpeaa)DE-He213 genes (dpeaa)DE-He213 Hemicellulose (dpeaa)DE-He213 Agro-industrial residues (dpeaa)DE-He213 Corrêa, Juliana Moço verfasserin aut Maller, Alexandre verfasserin aut Kadowaki, Marina Kimiko verfasserin aut da Conceição-Silva, José Luis verfasserin aut Gandra, Rinaldo Ferreira verfasserin aut Simão, Rita de Cássia Garcia verfasserin aut Enthalten in Antonie van Leeuwenhoek Dordrecht [u.a.] : Springer Science + Business Media B.V, 1934 108(2015), 4 vom: 12. Aug., Seite 993-1007 (DE-627)270929355 (DE-600)1478112-8 1572-9699 nnns volume:108 year:2015 number:4 day:12 month:08 pages:993-1007 https://dx.doi.org/10.1007/s10482-015-0552-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.30 ASE AR 108 2015 4 12 08 993-1007 |
| allfieldsSound |
10.1007/s10482-015-0552-x doi (DE-627)SPR01037891X (SPR)s10482-015-0552-x-e DE-627 ger DE-627 rakwb eng 570 610 ASE 42.30 bkl Justo, Priscila Innocenti verfasserin aut Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). To date, this is the first report to demonstrate the characterization of a GH3-BglX family member in C. crescentus that may have applications in biotechnological processes (i.e., the simultaneous saccharification process) because the multifunctional enzyme could play an important role in bacterial hemicellulose degradation. Cloning and expression (dpeaa)DE-He213 genes (dpeaa)DE-He213 Hemicellulose (dpeaa)DE-He213 Agro-industrial residues (dpeaa)DE-He213 Corrêa, Juliana Moço verfasserin aut Maller, Alexandre verfasserin aut Kadowaki, Marina Kimiko verfasserin aut da Conceição-Silva, José Luis verfasserin aut Gandra, Rinaldo Ferreira verfasserin aut Simão, Rita de Cássia Garcia verfasserin aut Enthalten in Antonie van Leeuwenhoek Dordrecht [u.a.] : Springer Science + Business Media B.V, 1934 108(2015), 4 vom: 12. Aug., Seite 993-1007 (DE-627)270929355 (DE-600)1478112-8 1572-9699 nnns volume:108 year:2015 number:4 day:12 month:08 pages:993-1007 https://dx.doi.org/10.1007/s10482-015-0552-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.30 ASE AR 108 2015 4 12 08 993-1007 |
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English |
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Enthalten in Antonie van Leeuwenhoek 108(2015), 4 vom: 12. Aug., Seite 993-1007 volume:108 year:2015 number:4 day:12 month:08 pages:993-1007 |
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Enthalten in Antonie van Leeuwenhoek 108(2015), 4 vom: 12. Aug., Seite 993-1007 volume:108 year:2015 number:4 day:12 month:08 pages:993-1007 |
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Cloning and expression genes Hemicellulose Agro-industrial residues |
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Antonie van Leeuwenhoek |
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Justo, Priscila Innocenti @@aut@@ Corrêa, Juliana Moço @@aut@@ Maller, Alexandre @@aut@@ Kadowaki, Marina Kimiko @@aut@@ da Conceição-Silva, José Luis @@aut@@ Gandra, Rinaldo Ferreira @@aut@@ Simão, Rita de Cássia Garcia @@aut@@ |
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2015-08-12T00:00:00Z |
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Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). 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Justo, Priscila Innocenti |
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Justo, Priscila Innocenti ddc 570 bkl 42.30 misc Cloning and expression misc genes misc Hemicellulose misc Agro-industrial residues Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus |
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570 610 ASE 42.30 bkl Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus Cloning and expression (dpeaa)DE-He213 genes (dpeaa)DE-He213 Hemicellulose (dpeaa)DE-He213 Agro-industrial residues (dpeaa)DE-He213 |
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Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus |
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Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus |
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Justo, Priscila Innocenti Corrêa, Juliana Moço Maller, Alexandre Kadowaki, Marina Kimiko da Conceição-Silva, José Luis Gandra, Rinaldo Ferreira Simão, Rita de Cássia Garcia |
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analysis of the xynb5 gene encoding a multifunctional gh3-bglx β-glucosidase-β-xylosidase-α-arabinosidase member in caulobacter crescentus |
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Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus |
| abstract |
Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). To date, this is the first report to demonstrate the characterization of a GH3-BglX family member in C. crescentus that may have applications in biotechnological processes (i.e., the simultaneous saccharification process) because the multifunctional enzyme could play an important role in bacterial hemicellulose degradation. |
| abstractGer |
Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). To date, this is the first report to demonstrate the characterization of a GH3-BglX family member in C. crescentus that may have applications in biotechnological processes (i.e., the simultaneous saccharification process) because the multifunctional enzyme could play an important role in bacterial hemicellulose degradation. |
| abstract_unstemmed |
Abstract The Caulobacter crescentus (NA1000) xynB5 gene (CCNA_03149) encodes a predicted β-glucosidase-β-xylosidase enzyme that was amplified by polymerase chain reaction; the product was cloned into the blunt ends of the pJet1.2 plasmid. Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. BglX-V-Ara predominantly presented β-glucosidase activity, with the highest affinity for its substrate and catalytic efficiency ($ K_{m} $ 0.24 ± 0.0005 mM, $ V_{max} $ 0.041 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.27 $ mM^{−1} $ $ s^{−1} $), followed by β-xylosidase ($ K_{m} $ 0.64 ± 0.032 mM, $ V_{max} $ 0.055 ± 0.002 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.14 $ mM^{−1} %$ s^{−1} $) and finally α-l-arabinosidase ($ K_{m} $ 1.45 ± 0.05 mM, $ V_{max} $ 0.091 ± 0.0004 µmol $ min^{−1} $ $ mg^{−1} $ and $ K_{cat} $/$ K_{m} $ 0.1 $ mM^{−1} $ $ s^{−1} $). To date, this is the first report to demonstrate the characterization of a GH3-BglX family member in C. crescentus that may have applications in biotechnological processes (i.e., the simultaneous saccharification process) because the multifunctional enzyme could play an important role in bacterial hemicellulose degradation. |
| collection_details |
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| container_issue |
4 |
| title_short |
Analysis of the xynB5 gene encoding a multifunctional GH3-BglX β-glucosidase-β-xylosidase-α-arabinosidase member in Caulobacter crescentus |
| url |
https://dx.doi.org/10.1007/s10482-015-0552-x |
| remote_bool |
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| author2 |
Corrêa, Juliana Moço Maller, Alexandre Kadowaki, Marina Kimiko da Conceição-Silva, José Luis Gandra, Rinaldo Ferreira Simão, Rita de Cássia Garcia |
| author2Str |
Corrêa, Juliana Moço Maller, Alexandre Kadowaki, Marina Kimiko da Conceição-Silva, José Luis Gandra, Rinaldo Ferreira Simão, Rita de Cássia Garcia |
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| doi_str |
10.1007/s10482-015-0552-x |
| up_date |
2024-07-03T15:45:11.434Z |
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1803573276378660864 |
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Analysis of the protein sequence indicated the presence of conserved glycosyl hydrolase 3 (GH3), β-glucosidase-related glycosidase (BglX) and fibronectin type III-like domains. After verifying its identity by DNA sequencing, the xynB5 gene was linked to an amino-terminal His-tag using the pTrcHisA vector. A recombinant protein (95 kDa) was successfully overexpressed from the xynB5 gene in E. coli Top 10 and purified using pre-packed nickel-Sepharose columns. The purified protein (BglX-V-Ara) demonstrated multifunctional activities in the presence of different substrates for β-glucosidase (pNPG: p-nitrophenyl-β-D-glucoside) β-xylosidase (pNPX: p-nitrophenyl-β-D-xyloside) and α-arabinosidase (pNPA: p-nitrophenyl-α-L-arabinosidase). BglX-V-Ara presented an optimal pH of 6 for all substrates and optimal temperature of 50 °C for β-glucosidase and α-l-arabinosidase and 60 °C for β-xylosidase. 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| score |
7.401017 |