Polyphenol Oxidase from Bean Sprouts (Glycine max L.)
: Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence...
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Gespeichert in:
| Autor*in: |
Nagai, T. [verfasserIn] Suzuki, N. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 2003 |
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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, 68(2003), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:68 ; year:2003 ; number:1 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1111/j.1365-2621.2003.tb14107.x |
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NLEJ243211198 |
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| 520 | |a : Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d. | ||
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10.1111/j.1365-2621.2003.tb14107.x doi (DE-627)NLEJ243211198 DE-627 ger DE-627 rakwb Nagai, T. verfasserin aut Polyphenol Oxidase from Bean Sprouts (Glycine max L.) Oxford, UK Blackwell Publishing Ltd 2003 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| polyphenol oxidase Suzuki, N. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 68(2003), 1, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:68 year:2003 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2003.tb14107.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 68 2003 1 0 |
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10.1111/j.1365-2621.2003.tb14107.x doi (DE-627)NLEJ243211198 DE-627 ger DE-627 rakwb Nagai, T. verfasserin aut Polyphenol Oxidase from Bean Sprouts (Glycine max L.) Oxford, UK Blackwell Publishing Ltd 2003 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| polyphenol oxidase Suzuki, N. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 68(2003), 1, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:68 year:2003 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2003.tb14107.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 68 2003 1 0 |
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10.1111/j.1365-2621.2003.tb14107.x doi (DE-627)NLEJ243211198 DE-627 ger DE-627 rakwb Nagai, T. verfasserin aut Polyphenol Oxidase from Bean Sprouts (Glycine max L.) Oxford, UK Blackwell Publishing Ltd 2003 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| polyphenol oxidase Suzuki, N. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 68(2003), 1, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:68 year:2003 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2003.tb14107.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 68 2003 1 0 |
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10.1111/j.1365-2621.2003.tb14107.x doi (DE-627)NLEJ243211198 DE-627 ger DE-627 rakwb Nagai, T. verfasserin aut Polyphenol Oxidase from Bean Sprouts (Glycine max L.) Oxford, UK Blackwell Publishing Ltd 2003 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| polyphenol oxidase Suzuki, N. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 68(2003), 1, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:68 year:2003 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2003.tb14107.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 68 2003 1 0 |
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10.1111/j.1365-2621.2003.tb14107.x doi (DE-627)NLEJ243211198 DE-627 ger DE-627 rakwb Nagai, T. verfasserin aut Polyphenol Oxidase from Bean Sprouts (Glycine max L.) Oxford, UK Blackwell Publishing Ltd 2003 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| polyphenol oxidase Suzuki, N. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 68(2003), 1, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:68 year:2003 number:1 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2003.tb14107.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 68 2003 1 0 |
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| abstract |
: Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d. |
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: Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d. |
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: Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d. |
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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">NLEJ243211198</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707174045.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s2003 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1365-2621.2003.tb14107.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ243211198</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">Nagai, T.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Polyphenol Oxidase from Bean Sprouts (Glycine max L.)</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">2003</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">: Polyphenol oxidase (PPO) was purified and characterized from bean sprouts by ammonium sulfate precipitation, DEAE-Toyopearl 650M, CM-Toyopearl 650M, SuperQ-Toyopearl 650S and QAE-Toyopearl 550C column chromatographies. Substrate staining of the crude extract on electrophoresis showed the presence of 2 isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be about 54 kDa. The optimum pH was 9.0 and optimum temperature 40 °C. Heat inactivation occurred about 30 °C. PPO showed activity to catechol, pyrogallol and dopamine. These compounds such as ascorbic acid, L-cysteine, 2-mercaptoethanol, and glutathione used was the effective inhibitor. Enzyme activity was maintained for 7 d at 4 °C but suddenly decreased after 8 d.</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">polyphenol oxidase</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Suzuki, N.</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 science</subfield><subfield code="d">Chicago, Ill. : Inst., 1990</subfield><subfield code="g">68(2003), 1, 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:68</subfield><subfield code="g">year:2003</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.1365-2621.2003.tb14107.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">68</subfield><subfield code="j">2003</subfield><subfield code="e">1</subfield><subfield code="h">0</subfield></datafield></record></collection>
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