Continuous Spectrophotometric Method for Determining Monophenolase and Diphenolase Activities of Pear Polyphenoloxidase
A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
ESPÍN, JUAN CARLOS [verfasserIn] MORALES, MERCEDES [verfasserIn] VARÓN, RAMÓN [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1996 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Journal of food science - Chicago, Ill. : Inst., 1990, 61(1996), 6, Seite 0 |
| Übergeordnetes Werk: |
volume:61 ; year:1996 ; number:6 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1111/j.1365-2621.1996.tb10955.x |
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| 520 | |a A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities. | ||
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10.1111/j.1365-2621.1996.tb10955.x doi (DE-627)NLEJ240425170 DE-627 ger DE-627 rakwb ESPÍN, JUAN CARLOS verfasserin aut Continuous Spectrophotometric Method for Determining Monophenolase and Diphenolase Activities of Pear Polyphenoloxidase Oxford, UK Blackwell Publishing Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| pear MORALES, MERCEDES verfasserin aut VARÓN, RAMÓN verfasserin aut TUDELA, JOSÉ oth GARCÍA-CÁNOVAS, FRANCISCO oth In Journal of food science Chicago, Ill. : Inst., 1990 61(1996), 6, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:61 year:1996 number:6 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1996.tb10955.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 61 1996 6 0 |
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10.1111/j.1365-2621.1996.tb10955.x doi (DE-627)NLEJ240425170 DE-627 ger DE-627 rakwb ESPÍN, JUAN CARLOS verfasserin aut Continuous Spectrophotometric Method for Determining Monophenolase and Diphenolase Activities of Pear Polyphenoloxidase Oxford, UK Blackwell Publishing Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| pear MORALES, MERCEDES verfasserin aut VARÓN, RAMÓN verfasserin aut TUDELA, JOSÉ oth GARCÍA-CÁNOVAS, FRANCISCO oth In Journal of food science Chicago, Ill. : Inst., 1990 61(1996), 6, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:61 year:1996 number:6 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1996.tb10955.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 61 1996 6 0 |
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10.1111/j.1365-2621.1996.tb10955.x doi (DE-627)NLEJ240425170 DE-627 ger DE-627 rakwb ESPÍN, JUAN CARLOS verfasserin aut Continuous Spectrophotometric Method for Determining Monophenolase and Diphenolase Activities of Pear Polyphenoloxidase Oxford, UK Blackwell Publishing Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| pear MORALES, MERCEDES verfasserin aut VARÓN, RAMÓN verfasserin aut TUDELA, JOSÉ oth GARCÍA-CÁNOVAS, FRANCISCO oth In Journal of food science Chicago, Ill. : Inst., 1990 61(1996), 6, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:61 year:1996 number:6 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1996.tb10955.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 61 1996 6 0 |
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10.1111/j.1365-2621.1996.tb10955.x doi (DE-627)NLEJ240425170 DE-627 ger DE-627 rakwb ESPÍN, JUAN CARLOS verfasserin aut Continuous Spectrophotometric Method for Determining Monophenolase and Diphenolase Activities of Pear Polyphenoloxidase Oxford, UK Blackwell Publishing Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| pear MORALES, MERCEDES verfasserin aut VARÓN, RAMÓN verfasserin aut TUDELA, JOSÉ oth GARCÍA-CÁNOVAS, FRANCISCO oth In Journal of food science Chicago, Ill. : Inst., 1990 61(1996), 6, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:61 year:1996 number:6 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1996.tb10955.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 61 1996 6 0 |
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10.1111/j.1365-2621.1996.tb10955.x doi (DE-627)NLEJ240425170 DE-627 ger DE-627 rakwb ESPÍN, JUAN CARLOS verfasserin aut Continuous Spectrophotometric Method for Determining Monophenolase and Diphenolase Activities of Pear Polyphenoloxidase Oxford, UK Blackwell Publishing Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| pear MORALES, MERCEDES verfasserin aut VARÓN, RAMÓN verfasserin aut TUDELA, JOSÉ oth GARCÍA-CÁNOVAS, FRANCISCO oth In Journal of food science Chicago, Ill. : Inst., 1990 61(1996), 6, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:61 year:1996 number:6 pages:0 http://dx.doi.org/10.1111/j.1365-2621.1996.tb10955.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 61 1996 6 0 |
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Continuous Spectrophotometric Method for Determining Monophenolase and Diphenolase Activities of Pear Polyphenoloxidase |
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A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities. |
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A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities. |
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A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities. |
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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">NLEJ240425170</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707111802.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1996 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1365-2621.1996.tb10955.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240425170</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">ESPÍN, JUAN CARLOS</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Continuous Spectrophotometric Method for Determining Monophenolase and Diphenolase Activities of Pear Polyphenoloxidase</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1996</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">A continuous spectrophotometric method was based on the coupling reaction between 3-methyl-2-benzothiazolinone hydrazone (MBTH) and the quinone product of the oxidation of p-hydroxyphenyl propionic acid (PHPPA) or 3,4-dihydroxyphenyl propionic acid (DHPPA) in the presence of polyphenol oxidase. The monophenolase activity of pear PPO was characterized for the first time. Solubility and stability of the adduct formed at the optimum pH (4.3) enabled the system to reach steady-state, making it possible to determine monophenolase activity with short lag periods. This, together with the value of ε for the MBTH-quinone adduct, makes this method more sensitive than other continuous methods for assaying monophenolase and diphenolase activities.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">pear</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">MORALES, MERCEDES</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">VARÓN, RAMÓN</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">TUDELA, JOSÉ</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">GARCÍA-CÁNOVAS, FRANCISCO</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of food science</subfield><subfield code="d">Chicago, Ill. : Inst., 1990</subfield><subfield code="g">61(1996), 6, Seite 0</subfield><subfield code="w">(DE-627)NLEJ243926316</subfield><subfield code="w">(DE-600)2006705-7</subfield><subfield code="x">1750-3841</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:61</subfield><subfield code="g">year:1996</subfield><subfield code="g">number:6</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.1365-2621.1996.tb10955.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">61</subfield><subfield code="j">1996</subfield><subfield code="e">6</subfield><subfield code="h">0</subfield></datafield></record></collection>
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