The influence of water activity on thermal stability of horseradish peroxidase
The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
HENDRICKX, M. [verfasserIn] SARAIVA, J. [verfasserIn] LYSSENS, J. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1992 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2007 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: International journal of food science & technology - Oxford [u.a.] : Wiley-Blackwell, 1987, 27(1992), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:27 ; year:1992 ; number:1 ; pages:0 |
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| DOI / URN: |
10.1111/j.1365-2621.1992.tb01175.x |
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| 520 | |a The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively). | ||
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10.1111/j.1365-2621.1992.tb01175.x doi (DE-627)NLEJ239419707 DE-627 ger DE-627 rakwb HENDRICKX, M. verfasserin aut The influence of water activity on thermal stability of horseradish peroxidase Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively). 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Decimal reduction time SARAIVA, J. verfasserin aut LYSSENS, J. verfasserin aut OLIVEIRA, J. oth TOBBACK, P. oth In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 27(1992), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:27 year:1992 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1992.tb01175.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 27 1992 1 0 |
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10.1111/j.1365-2621.1992.tb01175.x doi (DE-627)NLEJ239419707 DE-627 ger DE-627 rakwb HENDRICKX, M. verfasserin aut The influence of water activity on thermal stability of horseradish peroxidase Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively). 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Decimal reduction time SARAIVA, J. verfasserin aut LYSSENS, J. verfasserin aut OLIVEIRA, J. oth TOBBACK, P. oth In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 27(1992), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:27 year:1992 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1992.tb01175.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 27 1992 1 0 |
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10.1111/j.1365-2621.1992.tb01175.x doi (DE-627)NLEJ239419707 DE-627 ger DE-627 rakwb HENDRICKX, M. verfasserin aut The influence of water activity on thermal stability of horseradish peroxidase Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively). 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Decimal reduction time SARAIVA, J. verfasserin aut LYSSENS, J. verfasserin aut OLIVEIRA, J. oth TOBBACK, P. oth In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 27(1992), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:27 year:1992 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1992.tb01175.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 27 1992 1 0 |
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10.1111/j.1365-2621.1992.tb01175.x doi (DE-627)NLEJ239419707 DE-627 ger DE-627 rakwb HENDRICKX, M. verfasserin aut The influence of water activity on thermal stability of horseradish peroxidase Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively). 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Decimal reduction time SARAIVA, J. verfasserin aut LYSSENS, J. verfasserin aut OLIVEIRA, J. oth TOBBACK, P. oth In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 27(1992), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:27 year:1992 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1992.tb01175.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 27 1992 1 0 |
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10.1111/j.1365-2621.1992.tb01175.x doi (DE-627)NLEJ239419707 DE-627 ger DE-627 rakwb HENDRICKX, M. verfasserin aut The influence of water activity on thermal stability of horseradish peroxidase Oxford, UK Blackwell Publishing Ltd 1992 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively). 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| Decimal reduction time SARAIVA, J. verfasserin aut LYSSENS, J. verfasserin aut OLIVEIRA, J. oth TOBBACK, P. oth In International journal of food science & technology Oxford [u.a.] : Wiley-Blackwell, 1987 27(1992), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926502 (DE-600)2016518-3 1365-2621 nnns volume:27 year:1992 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1992.tb01175.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 27 1992 1 0 |
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The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively). |
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The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively). |
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The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively). |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ239419707</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707084840.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1992 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1365-2621.1992.tb01175.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ239419707</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">HENDRICKX, M.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">The influence of water activity on thermal stability of horseradish peroxidase</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1992</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively).</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2007</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2007||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Decimal reduction time</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">SARAIVA, J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">LYSSENS, J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">OLIVEIRA, J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">TOBBACK, P.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">International journal of food science & technology</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1987</subfield><subfield code="g">27(1992), 1, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243926502</subfield><subfield code="w">(DE-600)2016518-3</subfield><subfield code="x">1365-2621</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:27</subfield><subfield code="g">year:1992</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1365-2621.1992.tb01175.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">27</subfield><subfield code="j">1992</subfield><subfield code="e">1</subfield><subfield code="h">0</subfield></datafield></record></collection>
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7.4009514 |