A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases
Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from n...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Rose, Devin J. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2010 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer Science+Business Media, LLC 2010 |
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| Übergeordnetes Werk: |
Enthalten in: Food analytical methods - New York, NY : Springer, 2008, 4(2010), 1 vom: 19. Jan., Seite 66-72 |
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| Übergeordnetes Werk: |
volume:4 ; year:2010 ; number:1 ; day:19 ; month:01 ; pages:66-72 |
| Links: |
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| DOI / URN: |
10.1007/s12161-009-9121-0 |
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| Katalog-ID: |
SPR025451170 |
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| 100 | 1 | |a Rose, Devin J. |e verfasserin |4 aut | |
| 245 | 1 | 2 | |a A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases |
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| 520 | |a Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. Activity on substrates from different botanical origin differed by up to 100-fold, emphasizing the need for the use of application-specific substrates to obtain accurate estimations of enzyme activity. | ||
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| 650 | 4 | |a Arabinoxylan |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Inglett, George E. |4 aut | |
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10.1007/s12161-009-9121-0 doi (DE-627)SPR025451170 (SPR)s12161-009-9121-0-e DE-627 ger DE-627 rakwb eng Rose, Devin J. verfasserin aut A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2010 Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. Activity on substrates from different botanical origin differed by up to 100-fold, emphasizing the need for the use of application-specific substrates to obtain accurate estimations of enzyme activity. Bread (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Pentosan (dpeaa)DE-He213 Wheat (dpeaa)DE-He213 Arabinoxylan (dpeaa)DE-He213 Inglett, George E. aut Enthalten in Food analytical methods New York, NY : Springer, 2008 4(2010), 1 vom: 19. Jan., Seite 66-72 (DE-627)566007320 (DE-600)2424728-5 1936-976X nnns volume:4 year:2010 number:1 day:19 month:01 pages:66-72 https://dx.doi.org/10.1007/s12161-009-9121-0 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_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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 AR 4 2010 1 19 01 66-72 |
| spelling |
10.1007/s12161-009-9121-0 doi (DE-627)SPR025451170 (SPR)s12161-009-9121-0-e DE-627 ger DE-627 rakwb eng Rose, Devin J. verfasserin aut A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2010 Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. Activity on substrates from different botanical origin differed by up to 100-fold, emphasizing the need for the use of application-specific substrates to obtain accurate estimations of enzyme activity. Bread (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Pentosan (dpeaa)DE-He213 Wheat (dpeaa)DE-He213 Arabinoxylan (dpeaa)DE-He213 Inglett, George E. aut Enthalten in Food analytical methods New York, NY : Springer, 2008 4(2010), 1 vom: 19. Jan., Seite 66-72 (DE-627)566007320 (DE-600)2424728-5 1936-976X nnns volume:4 year:2010 number:1 day:19 month:01 pages:66-72 https://dx.doi.org/10.1007/s12161-009-9121-0 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_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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 AR 4 2010 1 19 01 66-72 |
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10.1007/s12161-009-9121-0 doi (DE-627)SPR025451170 (SPR)s12161-009-9121-0-e DE-627 ger DE-627 rakwb eng Rose, Devin J. verfasserin aut A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2010 Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. Activity on substrates from different botanical origin differed by up to 100-fold, emphasizing the need for the use of application-specific substrates to obtain accurate estimations of enzyme activity. Bread (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Pentosan (dpeaa)DE-He213 Wheat (dpeaa)DE-He213 Arabinoxylan (dpeaa)DE-He213 Inglett, George E. aut Enthalten in Food analytical methods New York, NY : Springer, 2008 4(2010), 1 vom: 19. Jan., Seite 66-72 (DE-627)566007320 (DE-600)2424728-5 1936-976X nnns volume:4 year:2010 number:1 day:19 month:01 pages:66-72 https://dx.doi.org/10.1007/s12161-009-9121-0 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_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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 AR 4 2010 1 19 01 66-72 |
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10.1007/s12161-009-9121-0 doi (DE-627)SPR025451170 (SPR)s12161-009-9121-0-e DE-627 ger DE-627 rakwb eng Rose, Devin J. verfasserin aut A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2010 Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. Activity on substrates from different botanical origin differed by up to 100-fold, emphasizing the need for the use of application-specific substrates to obtain accurate estimations of enzyme activity. Bread (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Pentosan (dpeaa)DE-He213 Wheat (dpeaa)DE-He213 Arabinoxylan (dpeaa)DE-He213 Inglett, George E. aut Enthalten in Food analytical methods New York, NY : Springer, 2008 4(2010), 1 vom: 19. Jan., Seite 66-72 (DE-627)566007320 (DE-600)2424728-5 1936-976X nnns volume:4 year:2010 number:1 day:19 month:01 pages:66-72 https://dx.doi.org/10.1007/s12161-009-9121-0 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_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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 AR 4 2010 1 19 01 66-72 |
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10.1007/s12161-009-9121-0 doi (DE-627)SPR025451170 (SPR)s12161-009-9121-0-e DE-627 ger DE-627 rakwb eng Rose, Devin J. verfasserin aut A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer Science+Business Media, LLC 2010 Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. Activity on substrates from different botanical origin differed by up to 100-fold, emphasizing the need for the use of application-specific substrates to obtain accurate estimations of enzyme activity. Bread (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Pentosan (dpeaa)DE-He213 Wheat (dpeaa)DE-He213 Arabinoxylan (dpeaa)DE-He213 Inglett, George E. aut Enthalten in Food analytical methods New York, NY : Springer, 2008 4(2010), 1 vom: 19. Jan., Seite 66-72 (DE-627)566007320 (DE-600)2424728-5 1936-976X nnns volume:4 year:2010 number:1 day:19 month:01 pages:66-72 https://dx.doi.org/10.1007/s12161-009-9121-0 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_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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 AR 4 2010 1 19 01 66-72 |
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Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. 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| author |
Rose, Devin J. |
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Rose, Devin J. misc Bread misc Enzyme misc Pentosan misc Wheat misc Arabinoxylan A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases |
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A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases Bread (dpeaa)DE-He213 Enzyme (dpeaa)DE-He213 Pentosan (dpeaa)DE-He213 Wheat (dpeaa)DE-He213 Arabinoxylan (dpeaa)DE-He213 |
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A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases |
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A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases |
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Rose, Devin J. |
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Food analytical methods |
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10.1007/s12161-009-9121-0 |
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method for the determination of soluble arabinoxylan released from insoluble substrates by xylanases |
| title_auth |
A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases |
| abstract |
Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. Activity on substrates from different botanical origin differed by up to 100-fold, emphasizing the need for the use of application-specific substrates to obtain accurate estimations of enzyme activity. © Springer Science+Business Media, LLC 2010 |
| abstractGer |
Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. Activity on substrates from different botanical origin differed by up to 100-fold, emphasizing the need for the use of application-specific substrates to obtain accurate estimations of enzyme activity. © Springer Science+Business Media, LLC 2010 |
| abstract_unstemmed |
Abstract The propensity for xylanase to convert insoluble to soluble arabinoxylan is an important parameter in many applications. Current methods for determining xylanase activity on insoluble substrates are nonspecific or utilize artificial substrates which may provide much different results from native substrates. Therefore, a new method for the determination of xylanase activity on insoluble substrates was developed. This method involved incubation of the enzyme with a material containing insoluble arabinoxylan. Arabinoxylan released by the enzyme was quantified as total pentose sugars colorimetrically by reaction with phloroglucinol upon heating in acetic–hydrochloric acid. Absorbance was determined at 552 nm, and interfering hexoses were accounted for by subtracting the absorbance at 510 nm. Because the method measured total pentose sugars released by the enzyme, (arabino)xylanase activity, rather than xylanase activity, was recommended for expressing results. The method was tested using two xylanases and six insoluble arabinoxylan-containing substrates. Sodium acetate and sodium citrate buffers (50 mM) were suitable for the reaction; sodium phosphate buffer substantially interfered with quantification of reaction products by reducing color development. The enzymic release of soluble arabinoxylan was linear for at least 5 min under all reaction conditions tested. Contaminating amylase and cellulase activity did not influence the results, despite the presence of starch and cellulose in many substrate sources. Relative standard deviations were <5% between reactions assayed on different days. Activity on substrates from different botanical origin differed by up to 100-fold, emphasizing the need for the use of application-specific substrates to obtain accurate estimations of enzyme activity. © Springer Science+Business Media, LLC 2010 |
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A Method for the Determination of Soluble Arabinoxylan Released from Insoluble Substrates by Xylanases |
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https://dx.doi.org/10.1007/s12161-009-9121-0 |
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| score |
7.402815 |