SIMULATION OF AN IMMOBILIZED ENZYME PARTICLE USING β-GALACTOSIDASE ADSORBED TO A PHENOL-FORMALDEHYDE RESIN
The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady s...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
GRULKE, ERIC A. [verfasserIn] OKOS, MARTIN R. [verfasserIn] SYVERSON, ALDRICH [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1977 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2007 ; Blackwell Publishing Journal Backfiles 1879-2005 |
|---|---|
| Übergeordnetes Werk: |
In: Journal of food process engineering - Oxford [u.a.] : Wiley-Blackwell, 1977, 1(1977), 4, Seite 0 |
| Übergeordnetes Werk: |
volume:1 ; year:1977 ; number:4 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1111/j.1745-4530.1977.tb00191.x |
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| 520 | |a The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading. | ||
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10.1111/j.1745-4530.1977.tb00191.x doi (DE-627)NLEJ240422112 DE-627 ger DE-627 rakwb GRULKE, ERIC A. verfasserin aut SIMULATION OF AN IMMOBILIZED ENZYME PARTICLE USING β-GALACTOSIDASE ADSORBED TO A PHENOL-FORMALDEHYDE RESIN Oxford, UK Blackwell Publishing Ltd 1977 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| OKOS, MARTIN R. verfasserin aut SYVERSON, ALDRICH verfasserin aut In Journal of food process engineering Oxford [u.a.] : Wiley-Blackwell, 1977 1(1977), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927029 (DE-600)2175259-X 1745-4530 nnns volume:1 year:1977 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4530.1977.tb00191.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 1 1977 4 0 |
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10.1111/j.1745-4530.1977.tb00191.x doi (DE-627)NLEJ240422112 DE-627 ger DE-627 rakwb GRULKE, ERIC A. verfasserin aut SIMULATION OF AN IMMOBILIZED ENZYME PARTICLE USING β-GALACTOSIDASE ADSORBED TO A PHENOL-FORMALDEHYDE RESIN Oxford, UK Blackwell Publishing Ltd 1977 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| OKOS, MARTIN R. verfasserin aut SYVERSON, ALDRICH verfasserin aut In Journal of food process engineering Oxford [u.a.] : Wiley-Blackwell, 1977 1(1977), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927029 (DE-600)2175259-X 1745-4530 nnns volume:1 year:1977 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4530.1977.tb00191.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 1 1977 4 0 |
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10.1111/j.1745-4530.1977.tb00191.x doi (DE-627)NLEJ240422112 DE-627 ger DE-627 rakwb GRULKE, ERIC A. verfasserin aut SIMULATION OF AN IMMOBILIZED ENZYME PARTICLE USING β-GALACTOSIDASE ADSORBED TO A PHENOL-FORMALDEHYDE RESIN Oxford, UK Blackwell Publishing Ltd 1977 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| OKOS, MARTIN R. verfasserin aut SYVERSON, ALDRICH verfasserin aut In Journal of food process engineering Oxford [u.a.] : Wiley-Blackwell, 1977 1(1977), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927029 (DE-600)2175259-X 1745-4530 nnns volume:1 year:1977 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4530.1977.tb00191.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 1 1977 4 0 |
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10.1111/j.1745-4530.1977.tb00191.x doi (DE-627)NLEJ240422112 DE-627 ger DE-627 rakwb GRULKE, ERIC A. verfasserin aut SIMULATION OF AN IMMOBILIZED ENZYME PARTICLE USING β-GALACTOSIDASE ADSORBED TO A PHENOL-FORMALDEHYDE RESIN Oxford, UK Blackwell Publishing Ltd 1977 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| OKOS, MARTIN R. verfasserin aut SYVERSON, ALDRICH verfasserin aut In Journal of food process engineering Oxford [u.a.] : Wiley-Blackwell, 1977 1(1977), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927029 (DE-600)2175259-X 1745-4530 nnns volume:1 year:1977 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4530.1977.tb00191.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 1 1977 4 0 |
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10.1111/j.1745-4530.1977.tb00191.x doi (DE-627)NLEJ240422112 DE-627 ger DE-627 rakwb GRULKE, ERIC A. verfasserin aut SIMULATION OF AN IMMOBILIZED ENZYME PARTICLE USING β-GALACTOSIDASE ADSORBED TO A PHENOL-FORMALDEHYDE RESIN Oxford, UK Blackwell Publishing Ltd 1977 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| OKOS, MARTIN R. verfasserin aut SYVERSON, ALDRICH verfasserin aut In Journal of food process engineering Oxford [u.a.] : Wiley-Blackwell, 1977 1(1977), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927029 (DE-600)2175259-X 1745-4530 nnns volume:1 year:1977 number:4 pages:0 http://dx.doi.org/10.1111/j.1745-4530.1977.tb00191.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 1 1977 4 0 |
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SIMULATION OF AN IMMOBILIZED ENZYME PARTICLE USING β-GALACTOSIDASE ADSORBED TO A PHENOL-FORMALDEHYDE RESIN |
| abstract |
The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading. |
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The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading. |
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The mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading. |
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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">NLEJ240422112</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707111736.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1977 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1745-4530.1977.tb00191.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240422112</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">GRULKE, ERIC A.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">SIMULATION OF AN IMMOBILIZED ENZYME PARTICLE USING β-GALACTOSIDASE ADSORBED TO A PHENOL-FORMALDEHYDE RESIN</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1977</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 mass transfer and kinetic properties of both soluble and immobilized β-galactosidase were investigated. A reversible enzyme kinetic model was found to best fit the soluble and immobilized enzymatic lactose hydrolysis. A finite difference model was used to simulate the steady state and unsteady state behavior of an immobilized enzyme particle. The performance of the catalyst in a stirred tank reactor was simulated by using the physical properties of the support with the kinetic model and varying the effective substrate diffusivity to fit the data. A sensitivity analysis was performed to evaluate the effect of particle size, diffusivity, external mass transfer coefficient and enzyme loading.</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="700" ind1="1" ind2=" "><subfield code="a">OKOS, MARTIN R.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">SYVERSON, ALDRICH</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of food process engineering</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1977</subfield><subfield code="g">1(1977), 4, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927029</subfield><subfield code="w">(DE-600)2175259-X</subfield><subfield code="x">1745-4530</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:1</subfield><subfield code="g">year:1977</subfield><subfield code="g">number:4</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.1745-4530.1977.tb00191.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">1</subfield><subfield code="j">1977</subfield><subfield code="e">4</subfield><subfield code="h">0</subfield></datafield></record></collection>
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7.40166 |