Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food

Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to h...
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Autor*in:	Panthi, Sandesh [verfasserIn] Choi, Yoon Seok [verfasserIn] Choi, Yun Hee [verfasserIn] Kim, MiRi [verfasserIn] Yoo, Jin Cheol [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2016

Schlagwörter:	Low molecular weight xylanase Thermodynamic characterization Xylooligosaccharides

Übergeordnetes Werk:	Enthalten in: Applied biochemistry and biotechnology - Berlin : Springer, 1976, 179(2016), 1 vom: 16. Jan., Seite 126-142
Übergeordnetes Werk:	volume:179 ; year:2016 ; number:1 ; day:16 ; month:01 ; pages:126-142

Links:	Volltext

DOI / URN:	10.1007/s12010-016-1983-1

Katalog-ID:	SPR023590556

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245	1	0	\|a Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food
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520			\|a Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to have a mass of ∼27 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and xylan zymography. The purified xylanase was optimally active at 50 °C and pH 6 and stable over a wide range of pH (4.5–12.5). The N-terminal amino acid sequence of xylanase was GIQQGDDGKL. The activation energy for beechwood xylan hydrolysis was 29.39 $ kJmol^{−1} $ with kcat value of 927.582 × $ 10^{2} $ $ s^{−1} $. Km and Vmax were 0.080 mg/ml and 794.63 mmol $ min^{−1} $ $ mg^{−1} $. The analysis of other thermodynamic parameters like ∆H, ∆G, ∆S, $ Q_{10} $, ∆$ G_{E-S} $, and ∆$ G_{E-T} $ also supported the spontaneous formation of products, greater hydrolytic efficiency, and feasibility of enzymatic reaction, which also ratifies the novelty of this xylanase. The enzyme was strongly activated by $ Zn^{2+} $ and inhibited by $ Cu^{2+} $. The principal hydrolyzed end-products of this xylanase are xylobiose, xylotriose, and xylotetrose, which can be used in the pharmaceutical industry and as prebiotic in food.
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700	1		\|a Choi, Yun Hee \|e verfasserin \|4 aut
700	1		\|a Kim, MiRi \|e verfasserin \|4 aut
700	1		\|a Yoo, Jin Cheol \|e verfasserin \|4 aut
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912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_120
912			\|a GBV_ILN_138
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_152
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
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912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
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912			\|a GBV_ILN_281
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
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912			\|a GBV_ILN_2038
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912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2070
912			\|a GBV_ILN_2086
912			\|a GBV_ILN_2093
912			\|a GBV_ILN_2106
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allfields	10.1007/s12010-016-1983-1 doi (DE-627)SPR023590556 (SPR)s12010-016-1983-1-e DE-627 ger DE-627 rakwb eng 570 660 ASE 540 660 ASE Panthi, Sandesh verfasserin aut Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to have a mass of ∼27 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and xylan zymography. The purified xylanase was optimally active at 50 °C and pH 6 and stable over a wide range of pH (4.5–12.5). The N-terminal amino acid sequence of xylanase was GIQQGDDGKL. The activation energy for beechwood xylan hydrolysis was 29.39 $ kJmol^{−1} $ with kcat value of 927.582 × $ 10^{2} $ $ s^{−1} $. Km and Vmax were 0.080 mg/ml and 794.63 mmol $ min^{−1} $ $ mg^{−1} $. The analysis of other thermodynamic parameters like ∆H, ∆G, ∆S, $ Q_{10} $, ∆$ G_{E-S} $, and ∆$ G_{E-T} $ also supported the spontaneous formation of products, greater hydrolytic efficiency, and feasibility of enzymatic reaction, which also ratifies the novelty of this xylanase. The enzyme was strongly activated by $ Zn^{2+} $ and inhibited by $ Cu^{2+} $. The principal hydrolyzed end-products of this xylanase are xylobiose, xylotriose, and xylotetrose, which can be used in the pharmaceutical industry and as prebiotic in food. Low molecular weight xylanase (dpeaa)DE-He213 Thermodynamic characterization (dpeaa)DE-He213 Xylooligosaccharides (dpeaa)DE-He213 Choi, Yoon Seok verfasserin aut Choi, Yun Hee verfasserin aut Kim, MiRi verfasserin aut Yoo, Jin Cheol verfasserin aut Enthalten in Applied biochemistry and biotechnology Berlin : Springer, 1976 179(2016), 1 vom: 16. Jan., Seite 126-142 (DE-627)342894846 (DE-600)2072711-2 1559-0291 nnns volume:179 year:2016 number:1 day:16 month:01 pages:126-142 https://dx.doi.org/10.1007/s12010-016-1983-1 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_65 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_152 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_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_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_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_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 179 2016 1 16 01 126-142
spelling	10.1007/s12010-016-1983-1 doi (DE-627)SPR023590556 (SPR)s12010-016-1983-1-e DE-627 ger DE-627 rakwb eng 570 660 ASE 540 660 ASE Panthi, Sandesh verfasserin aut Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to have a mass of ∼27 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and xylan zymography. The purified xylanase was optimally active at 50 °C and pH 6 and stable over a wide range of pH (4.5–12.5). The N-terminal amino acid sequence of xylanase was GIQQGDDGKL. The activation energy for beechwood xylan hydrolysis was 29.39 $ kJmol^{−1} $ with kcat value of 927.582 × $ 10^{2} $ $ s^{−1} $. Km and Vmax were 0.080 mg/ml and 794.63 mmol $ min^{−1} $ $ mg^{−1} $. The analysis of other thermodynamic parameters like ∆H, ∆G, ∆S, $ Q_{10} $, ∆$ G_{E-S} $, and ∆$ G_{E-T} $ also supported the spontaneous formation of products, greater hydrolytic efficiency, and feasibility of enzymatic reaction, which also ratifies the novelty of this xylanase. The enzyme was strongly activated by $ Zn^{2+} $ and inhibited by $ Cu^{2+} $. The principal hydrolyzed end-products of this xylanase are xylobiose, xylotriose, and xylotetrose, which can be used in the pharmaceutical industry and as prebiotic in food. Low molecular weight xylanase (dpeaa)DE-He213 Thermodynamic characterization (dpeaa)DE-He213 Xylooligosaccharides (dpeaa)DE-He213 Choi, Yoon Seok verfasserin aut Choi, Yun Hee verfasserin aut Kim, MiRi verfasserin aut Yoo, Jin Cheol verfasserin aut Enthalten in Applied biochemistry and biotechnology Berlin : Springer, 1976 179(2016), 1 vom: 16. Jan., Seite 126-142 (DE-627)342894846 (DE-600)2072711-2 1559-0291 nnns volume:179 year:2016 number:1 day:16 month:01 pages:126-142 https://dx.doi.org/10.1007/s12010-016-1983-1 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_65 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_152 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_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_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_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_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 179 2016 1 16 01 126-142
allfields_unstemmed	10.1007/s12010-016-1983-1 doi (DE-627)SPR023590556 (SPR)s12010-016-1983-1-e DE-627 ger DE-627 rakwb eng 570 660 ASE 540 660 ASE Panthi, Sandesh verfasserin aut Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to have a mass of ∼27 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and xylan zymography. The purified xylanase was optimally active at 50 °C and pH 6 and stable over a wide range of pH (4.5–12.5). The N-terminal amino acid sequence of xylanase was GIQQGDDGKL. The activation energy for beechwood xylan hydrolysis was 29.39 $ kJmol^{−1} $ with kcat value of 927.582 × $ 10^{2} $ $ s^{−1} $. Km and Vmax were 0.080 mg/ml and 794.63 mmol $ min^{−1} $ $ mg^{−1} $. The analysis of other thermodynamic parameters like ∆H, ∆G, ∆S, $ Q_{10} $, ∆$ G_{E-S} $, and ∆$ G_{E-T} $ also supported the spontaneous formation of products, greater hydrolytic efficiency, and feasibility of enzymatic reaction, which also ratifies the novelty of this xylanase. The enzyme was strongly activated by $ Zn^{2+} $ and inhibited by $ Cu^{2+} $. The principal hydrolyzed end-products of this xylanase are xylobiose, xylotriose, and xylotetrose, which can be used in the pharmaceutical industry and as prebiotic in food. Low molecular weight xylanase (dpeaa)DE-He213 Thermodynamic characterization (dpeaa)DE-He213 Xylooligosaccharides (dpeaa)DE-He213 Choi, Yoon Seok verfasserin aut Choi, Yun Hee verfasserin aut Kim, MiRi verfasserin aut Yoo, Jin Cheol verfasserin aut Enthalten in Applied biochemistry and biotechnology Berlin : Springer, 1976 179(2016), 1 vom: 16. Jan., Seite 126-142 (DE-627)342894846 (DE-600)2072711-2 1559-0291 nnns volume:179 year:2016 number:1 day:16 month:01 pages:126-142 https://dx.doi.org/10.1007/s12010-016-1983-1 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_65 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_152 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_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_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_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_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 179 2016 1 16 01 126-142
allfieldsGer	10.1007/s12010-016-1983-1 doi (DE-627)SPR023590556 (SPR)s12010-016-1983-1-e DE-627 ger DE-627 rakwb eng 570 660 ASE 540 660 ASE Panthi, Sandesh verfasserin aut Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to have a mass of ∼27 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and xylan zymography. The purified xylanase was optimally active at 50 °C and pH 6 and stable over a wide range of pH (4.5–12.5). The N-terminal amino acid sequence of xylanase was GIQQGDDGKL. The activation energy for beechwood xylan hydrolysis was 29.39 $ kJmol^{−1} $ with kcat value of 927.582 × $ 10^{2} $ $ s^{−1} $. Km and Vmax were 0.080 mg/ml and 794.63 mmol $ min^{−1} $ $ mg^{−1} $. The analysis of other thermodynamic parameters like ∆H, ∆G, ∆S, $ Q_{10} $, ∆$ G_{E-S} $, and ∆$ G_{E-T} $ also supported the spontaneous formation of products, greater hydrolytic efficiency, and feasibility of enzymatic reaction, which also ratifies the novelty of this xylanase. The enzyme was strongly activated by $ Zn^{2+} $ and inhibited by $ Cu^{2+} $. The principal hydrolyzed end-products of this xylanase are xylobiose, xylotriose, and xylotetrose, which can be used in the pharmaceutical industry and as prebiotic in food. Low molecular weight xylanase (dpeaa)DE-He213 Thermodynamic characterization (dpeaa)DE-He213 Xylooligosaccharides (dpeaa)DE-He213 Choi, Yoon Seok verfasserin aut Choi, Yun Hee verfasserin aut Kim, MiRi verfasserin aut Yoo, Jin Cheol verfasserin aut Enthalten in Applied biochemistry and biotechnology Berlin : Springer, 1976 179(2016), 1 vom: 16. Jan., Seite 126-142 (DE-627)342894846 (DE-600)2072711-2 1559-0291 nnns volume:179 year:2016 number:1 day:16 month:01 pages:126-142 https://dx.doi.org/10.1007/s12010-016-1983-1 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_65 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_152 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_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_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_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_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 179 2016 1 16 01 126-142
allfieldsSound	10.1007/s12010-016-1983-1 doi (DE-627)SPR023590556 (SPR)s12010-016-1983-1-e DE-627 ger DE-627 rakwb eng 570 660 ASE 540 660 ASE Panthi, Sandesh verfasserin aut Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to have a mass of ∼27 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and xylan zymography. The purified xylanase was optimally active at 50 °C and pH 6 and stable over a wide range of pH (4.5–12.5). The N-terminal amino acid sequence of xylanase was GIQQGDDGKL. The activation energy for beechwood xylan hydrolysis was 29.39 $ kJmol^{−1} $ with kcat value of 927.582 × $ 10^{2} $ $ s^{−1} $. Km and Vmax were 0.080 mg/ml and 794.63 mmol $ min^{−1} $ $ mg^{−1} $. The analysis of other thermodynamic parameters like ∆H, ∆G, ∆S, $ Q_{10} $, ∆$ G_{E-S} $, and ∆$ G_{E-T} $ also supported the spontaneous formation of products, greater hydrolytic efficiency, and feasibility of enzymatic reaction, which also ratifies the novelty of this xylanase. The enzyme was strongly activated by $ Zn^{2+} $ and inhibited by $ Cu^{2+} $. The principal hydrolyzed end-products of this xylanase are xylobiose, xylotriose, and xylotetrose, which can be used in the pharmaceutical industry and as prebiotic in food. Low molecular weight xylanase (dpeaa)DE-He213 Thermodynamic characterization (dpeaa)DE-He213 Xylooligosaccharides (dpeaa)DE-He213 Choi, Yoon Seok verfasserin aut Choi, Yun Hee verfasserin aut Kim, MiRi verfasserin aut Yoo, Jin Cheol verfasserin aut Enthalten in Applied biochemistry and biotechnology Berlin : Springer, 1976 179(2016), 1 vom: 16. Jan., Seite 126-142 (DE-627)342894846 (DE-600)2072711-2 1559-0291 nnns volume:179 year:2016 number:1 day:16 month:01 pages:126-142 https://dx.doi.org/10.1007/s12010-016-1983-1 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_65 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_152 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_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_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_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_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 179 2016 1 16 01 126-142
language	English
source	Enthalten in Applied biochemistry and biotechnology 179(2016), 1 vom: 16. Jan., Seite 126-142 volume:179 year:2016 number:1 day:16 month:01 pages:126-142
sourceStr	Enthalten in Applied biochemistry and biotechnology 179(2016), 1 vom: 16. Jan., Seite 126-142 volume:179 year:2016 number:1 day:16 month:01 pages:126-142
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Low molecular weight xylanase Thermodynamic characterization Xylooligosaccharides
dewey-raw	570
isfreeaccess_bool	false
container_title	Applied biochemistry and biotechnology
authorswithroles_txt_mv	Panthi, Sandesh @@aut@@ Choi, Yoon Seok @@aut@@ Choi, Yun Hee @@aut@@ Kim, MiRi @@aut@@ Yoo, Jin Cheol @@aut@@
publishDateDaySort_date	2016-01-16T00:00:00Z
hierarchy_top_id	342894846
dewey-sort	3570
id	SPR023590556
language_de	englisch
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author	Panthi, Sandesh
spellingShingle	Panthi, Sandesh ddc 570 ddc 540 misc Low molecular weight xylanase misc Thermodynamic characterization misc Xylooligosaccharides Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food
authorStr	Panthi, Sandesh
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topic_title	570 660 ASE 540 660 ASE Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food Low molecular weight xylanase (dpeaa)DE-He213 Thermodynamic characterization (dpeaa)DE-He213 Xylooligosaccharides (dpeaa)DE-He213
topic	ddc 570 ddc 540 misc Low molecular weight xylanase misc Thermodynamic characterization misc Xylooligosaccharides
topic_unstemmed	ddc 570 ddc 540 misc Low molecular weight xylanase misc Thermodynamic characterization misc Xylooligosaccharides
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title	Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food
ctrlnum	(DE-627)SPR023590556 (SPR)s12010-016-1983-1-e
title_full	Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food
author_sort	Panthi, Sandesh
journal	Applied biochemistry and biotechnology
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author_browse	Panthi, Sandesh Choi, Yoon Seok Choi, Yun Hee Kim, MiRi Yoo, Jin Cheol
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author-letter	Panthi, Sandesh
doi_str_mv	10.1007/s12010-016-1983-1
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title_sort	biochemical and thermodynamic characterization of a novel, low molecular weight xylanase from bacillus methylotrophicus csb40 isolated from traditional korean food
title_auth	Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food
abstract	Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to have a mass of ∼27 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and xylan zymography. The purified xylanase was optimally active at 50 °C and pH 6 and stable over a wide range of pH (4.5–12.5). The N-terminal amino acid sequence of xylanase was GIQQGDDGKL. The activation energy for beechwood xylan hydrolysis was 29.39 $ kJmol^{−1} $ with kcat value of 927.582 × $ 10^{2} $ $ s^{−1} $. Km and Vmax were 0.080 mg/ml and 794.63 mmol $ min^{−1} $ $ mg^{−1} $. The analysis of other thermodynamic parameters like ∆H, ∆G, ∆S, $ Q_{10} $, ∆$ G_{E-S} $, and ∆$ G_{E-T} $ also supported the spontaneous formation of products, greater hydrolytic efficiency, and feasibility of enzymatic reaction, which also ratifies the novelty of this xylanase. The enzyme was strongly activated by $ Zn^{2+} $ and inhibited by $ Cu^{2+} $. The principal hydrolyzed end-products of this xylanase are xylobiose, xylotriose, and xylotetrose, which can be used in the pharmaceutical industry and as prebiotic in food.
abstractGer	Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to have a mass of ∼27 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and xylan zymography. The purified xylanase was optimally active at 50 °C and pH 6 and stable over a wide range of pH (4.5–12.5). The N-terminal amino acid sequence of xylanase was GIQQGDDGKL. The activation energy for beechwood xylan hydrolysis was 29.39 $ kJmol^{−1} $ with kcat value of 927.582 × $ 10^{2} $ $ s^{−1} $. Km and Vmax were 0.080 mg/ml and 794.63 mmol $ min^{−1} $ $ mg^{−1} $. The analysis of other thermodynamic parameters like ∆H, ∆G, ∆S, $ Q_{10} $, ∆$ G_{E-S} $, and ∆$ G_{E-T} $ also supported the spontaneous formation of products, greater hydrolytic efficiency, and feasibility of enzymatic reaction, which also ratifies the novelty of this xylanase. The enzyme was strongly activated by $ Zn^{2+} $ and inhibited by $ Cu^{2+} $. The principal hydrolyzed end-products of this xylanase are xylobiose, xylotriose, and xylotetrose, which can be used in the pharmaceutical industry and as prebiotic in food.
abstract_unstemmed	Abstract A low molecular weight xylanase from Bacillus strain CSB40, isolated from traditional Korean food and produced in beechwood xylan, was biochemically and thermodynamically characterized. It was purified 8.12-fold with a 15.88 % yield using DEAE sepharose fast flow, and it was determined to have a mass of ∼27 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and xylan zymography. The purified xylanase was optimally active at 50 °C and pH 6 and stable over a wide range of pH (4.5–12.5). The N-terminal amino acid sequence of xylanase was GIQQGDDGKL. The activation energy for beechwood xylan hydrolysis was 29.39 $ kJmol^{−1} $ with kcat value of 927.582 × $ 10^{2} $ $ s^{−1} $. Km and Vmax were 0.080 mg/ml and 794.63 mmol $ min^{−1} $ $ mg^{−1} $. The analysis of other thermodynamic parameters like ∆H, ∆G, ∆S, $ Q_{10} $, ∆$ G_{E-S} $, and ∆$ G_{E-T} $ also supported the spontaneous formation of products, greater hydrolytic efficiency, and feasibility of enzymatic reaction, which also ratifies the novelty of this xylanase. The enzyme was strongly activated by $ Zn^{2+} $ and inhibited by $ Cu^{2+} $. The principal hydrolyzed end-products of this xylanase are xylobiose, xylotriose, and xylotetrose, which can be used in the pharmaceutical industry and as prebiotic in food.
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container_issue	1
title_short	Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food
url	https://dx.doi.org/10.1007/s12010-016-1983-1
remote_bool	true
author2	Choi, Yoon Seok Choi, Yun Hee Kim, MiRi Yoo, Jin Cheol
author2Str	Choi, Yoon Seok Choi, Yun Hee Kim, MiRi Yoo, Jin Cheol
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doi_str	10.1007/s12010-016-1983-1
up_date	2024-07-03T19:55:44.039Z
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Biochemical and Thermodynamic Characterization of a Novel, Low Molecular Weight Xylanase from Bacillus Methylotrophicus CSB40 Isolated from Traditional Korean Food

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