Space-time distribution of γ-glutamyl transferase activity in Agaricus bisporus
γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrat...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Jolivet, Sylvie [verfasserIn] Mooibroek, Hans [verfasserIn] Wichers, Harry J. [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1998 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
|---|---|
| Übergeordnetes Werk: |
In: FEMS microbiology letters - Federation of European Microbiological Societies ; GKD-ID: 114439X, Oxford [u.a.] : Wiley-Blackwell, 1977, 163(1998), 2, Seite 0 |
| Übergeordnetes Werk: |
volume:163 ; year:1998 ; number:2 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1111/j.1574-6968.1998.tb13055.x |
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NLEJ242912117 |
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| 520 | |a γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrated to be one of the main substrates implicated in mushroom browning. γ-G;utamyl transferase activity was measured in various tissues of A. bisporus fruitbodies at different developmental stages and in mycelium grown on synthetic and compost media. Gills and skin, which exhibit the highest levels of γ-glutamyl amino acids, also present the highest levels of γ-glutamyl transferase activity. Stipe base tissue, which is characterised by a lack of agaritine and the presence of its hydrolysis product hydroxymethylphenylhydrazine, also exhibits high levels of γ-glutamyl transferase activity. Thus, in the gills and in the skin, γ-glutamyl transferase could be mainly involved in the synthesis of γ-glutamyl derivatives and, in the stipe base, in the hydrolysis of agaritine. γ-Glutamyl transferase activity measured in mycelia was rather low but significantly greater in mycelium grown on compost medium than on synthetic medium. These results are in agreement with the lack of γ-glutaminyl-4-hydroxybenzene in mycelium grown on artificial medium. Cap flesh and stipe tissues show the lowest γ-glutamyl transferase activity. The elucidation of the role of γ-glutamyl transferase in the synthesis of one of the main substrates for mushroom browning opens new perspectives in attempts to optimise post-harvest quality. | ||
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10.1111/j.1574-6968.1998.tb13055.x doi (DE-627)NLEJ242912117 DE-627 ger DE-627 rakwb Jolivet, Sylvie verfasserin aut Space-time distribution of γ-glutamyl transferase activity in Agaricus bisporus Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrated to be one of the main substrates implicated in mushroom browning. γ-G;utamyl transferase activity was measured in various tissues of A. bisporus fruitbodies at different developmental stages and in mycelium grown on synthetic and compost media. Gills and skin, which exhibit the highest levels of γ-glutamyl amino acids, also present the highest levels of γ-glutamyl transferase activity. Stipe base tissue, which is characterised by a lack of agaritine and the presence of its hydrolysis product hydroxymethylphenylhydrazine, also exhibits high levels of γ-glutamyl transferase activity. Thus, in the gills and in the skin, γ-glutamyl transferase could be mainly involved in the synthesis of γ-glutamyl derivatives and, in the stipe base, in the hydrolysis of agaritine. γ-Glutamyl transferase activity measured in mycelia was rather low but significantly greater in mycelium grown on compost medium than on synthetic medium. These results are in agreement with the lack of γ-glutaminyl-4-hydroxybenzene in mycelium grown on artificial medium. Cap flesh and stipe tissues show the lowest γ-glutamyl transferase activity. The elucidation of the role of γ-glutamyl transferase in the synthesis of one of the main substrates for mushroom browning opens new perspectives in attempts to optimise post-harvest quality. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Mooibroek, Hans verfasserin aut Wichers, Harry J. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 163(1998), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:163 year:1998 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1998.tb13055.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 163 1998 2 0 |
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10.1111/j.1574-6968.1998.tb13055.x doi (DE-627)NLEJ242912117 DE-627 ger DE-627 rakwb Jolivet, Sylvie verfasserin aut Space-time distribution of γ-glutamyl transferase activity in Agaricus bisporus Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrated to be one of the main substrates implicated in mushroom browning. γ-G;utamyl transferase activity was measured in various tissues of A. bisporus fruitbodies at different developmental stages and in mycelium grown on synthetic and compost media. Gills and skin, which exhibit the highest levels of γ-glutamyl amino acids, also present the highest levels of γ-glutamyl transferase activity. Stipe base tissue, which is characterised by a lack of agaritine and the presence of its hydrolysis product hydroxymethylphenylhydrazine, also exhibits high levels of γ-glutamyl transferase activity. Thus, in the gills and in the skin, γ-glutamyl transferase could be mainly involved in the synthesis of γ-glutamyl derivatives and, in the stipe base, in the hydrolysis of agaritine. γ-Glutamyl transferase activity measured in mycelia was rather low but significantly greater in mycelium grown on compost medium than on synthetic medium. These results are in agreement with the lack of γ-glutaminyl-4-hydroxybenzene in mycelium grown on artificial medium. Cap flesh and stipe tissues show the lowest γ-glutamyl transferase activity. The elucidation of the role of γ-glutamyl transferase in the synthesis of one of the main substrates for mushroom browning opens new perspectives in attempts to optimise post-harvest quality. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Mooibroek, Hans verfasserin aut Wichers, Harry J. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 163(1998), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:163 year:1998 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1998.tb13055.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 163 1998 2 0 |
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10.1111/j.1574-6968.1998.tb13055.x doi (DE-627)NLEJ242912117 DE-627 ger DE-627 rakwb Jolivet, Sylvie verfasserin aut Space-time distribution of γ-glutamyl transferase activity in Agaricus bisporus Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrated to be one of the main substrates implicated in mushroom browning. γ-G;utamyl transferase activity was measured in various tissues of A. bisporus fruitbodies at different developmental stages and in mycelium grown on synthetic and compost media. Gills and skin, which exhibit the highest levels of γ-glutamyl amino acids, also present the highest levels of γ-glutamyl transferase activity. Stipe base tissue, which is characterised by a lack of agaritine and the presence of its hydrolysis product hydroxymethylphenylhydrazine, also exhibits high levels of γ-glutamyl transferase activity. Thus, in the gills and in the skin, γ-glutamyl transferase could be mainly involved in the synthesis of γ-glutamyl derivatives and, in the stipe base, in the hydrolysis of agaritine. γ-Glutamyl transferase activity measured in mycelia was rather low but significantly greater in mycelium grown on compost medium than on synthetic medium. These results are in agreement with the lack of γ-glutaminyl-4-hydroxybenzene in mycelium grown on artificial medium. Cap flesh and stipe tissues show the lowest γ-glutamyl transferase activity. The elucidation of the role of γ-glutamyl transferase in the synthesis of one of the main substrates for mushroom browning opens new perspectives in attempts to optimise post-harvest quality. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Mooibroek, Hans verfasserin aut Wichers, Harry J. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 163(1998), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:163 year:1998 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1998.tb13055.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 163 1998 2 0 |
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10.1111/j.1574-6968.1998.tb13055.x doi (DE-627)NLEJ242912117 DE-627 ger DE-627 rakwb Jolivet, Sylvie verfasserin aut Space-time distribution of γ-glutamyl transferase activity in Agaricus bisporus Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrated to be one of the main substrates implicated in mushroom browning. γ-G;utamyl transferase activity was measured in various tissues of A. bisporus fruitbodies at different developmental stages and in mycelium grown on synthetic and compost media. Gills and skin, which exhibit the highest levels of γ-glutamyl amino acids, also present the highest levels of γ-glutamyl transferase activity. Stipe base tissue, which is characterised by a lack of agaritine and the presence of its hydrolysis product hydroxymethylphenylhydrazine, also exhibits high levels of γ-glutamyl transferase activity. Thus, in the gills and in the skin, γ-glutamyl transferase could be mainly involved in the synthesis of γ-glutamyl derivatives and, in the stipe base, in the hydrolysis of agaritine. γ-Glutamyl transferase activity measured in mycelia was rather low but significantly greater in mycelium grown on compost medium than on synthetic medium. These results are in agreement with the lack of γ-glutaminyl-4-hydroxybenzene in mycelium grown on artificial medium. Cap flesh and stipe tissues show the lowest γ-glutamyl transferase activity. The elucidation of the role of γ-glutamyl transferase in the synthesis of one of the main substrates for mushroom browning opens new perspectives in attempts to optimise post-harvest quality. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Mooibroek, Hans verfasserin aut Wichers, Harry J. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 163(1998), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:163 year:1998 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1998.tb13055.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 163 1998 2 0 |
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10.1111/j.1574-6968.1998.tb13055.x doi (DE-627)NLEJ242912117 DE-627 ger DE-627 rakwb Jolivet, Sylvie verfasserin aut Space-time distribution of γ-glutamyl transferase activity in Agaricus bisporus Oxford, UK Blackwell Publishing Ltd 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrated to be one of the main substrates implicated in mushroom browning. γ-G;utamyl transferase activity was measured in various tissues of A. bisporus fruitbodies at different developmental stages and in mycelium grown on synthetic and compost media. Gills and skin, which exhibit the highest levels of γ-glutamyl amino acids, also present the highest levels of γ-glutamyl transferase activity. Stipe base tissue, which is characterised by a lack of agaritine and the presence of its hydrolysis product hydroxymethylphenylhydrazine, also exhibits high levels of γ-glutamyl transferase activity. Thus, in the gills and in the skin, γ-glutamyl transferase could be mainly involved in the synthesis of γ-glutamyl derivatives and, in the stipe base, in the hydrolysis of agaritine. γ-Glutamyl transferase activity measured in mycelia was rather low but significantly greater in mycelium grown on compost medium than on synthetic medium. These results are in agreement with the lack of γ-glutaminyl-4-hydroxybenzene in mycelium grown on artificial medium. Cap flesh and stipe tissues show the lowest γ-glutamyl transferase activity. The elucidation of the role of γ-glutamyl transferase in the synthesis of one of the main substrates for mushroom browning opens new perspectives in attempts to optimise post-harvest quality. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Mooibroek, Hans verfasserin aut Wichers, Harry J. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 163(1998), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:163 year:1998 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1998.tb13055.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 163 1998 2 0 |
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Space-time distribution of γ-glutamyl transferase activity in Agaricus bisporus |
| abstract |
γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrated to be one of the main substrates implicated in mushroom browning. γ-G;utamyl transferase activity was measured in various tissues of A. bisporus fruitbodies at different developmental stages and in mycelium grown on synthetic and compost media. Gills and skin, which exhibit the highest levels of γ-glutamyl amino acids, also present the highest levels of γ-glutamyl transferase activity. Stipe base tissue, which is characterised by a lack of agaritine and the presence of its hydrolysis product hydroxymethylphenylhydrazine, also exhibits high levels of γ-glutamyl transferase activity. Thus, in the gills and in the skin, γ-glutamyl transferase could be mainly involved in the synthesis of γ-glutamyl derivatives and, in the stipe base, in the hydrolysis of agaritine. γ-Glutamyl transferase activity measured in mycelia was rather low but significantly greater in mycelium grown on compost medium than on synthetic medium. These results are in agreement with the lack of γ-glutaminyl-4-hydroxybenzene in mycelium grown on artificial medium. Cap flesh and stipe tissues show the lowest γ-glutamyl transferase activity. The elucidation of the role of γ-glutamyl transferase in the synthesis of one of the main substrates for mushroom browning opens new perspectives in attempts to optimise post-harvest quality. |
| abstractGer |
γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrated to be one of the main substrates implicated in mushroom browning. γ-G;utamyl transferase activity was measured in various tissues of A. bisporus fruitbodies at different developmental stages and in mycelium grown on synthetic and compost media. Gills and skin, which exhibit the highest levels of γ-glutamyl amino acids, also present the highest levels of γ-glutamyl transferase activity. Stipe base tissue, which is characterised by a lack of agaritine and the presence of its hydrolysis product hydroxymethylphenylhydrazine, also exhibits high levels of γ-glutamyl transferase activity. Thus, in the gills and in the skin, γ-glutamyl transferase could be mainly involved in the synthesis of γ-glutamyl derivatives and, in the stipe base, in the hydrolysis of agaritine. γ-Glutamyl transferase activity measured in mycelia was rather low but significantly greater in mycelium grown on compost medium than on synthetic medium. These results are in agreement with the lack of γ-glutaminyl-4-hydroxybenzene in mycelium grown on artificial medium. Cap flesh and stipe tissues show the lowest γ-glutamyl transferase activity. The elucidation of the role of γ-glutamyl transferase in the synthesis of one of the main substrates for mushroom browning opens new perspectives in attempts to optimise post-harvest quality. |
| abstract_unstemmed |
γ-Glutamyl transferase is involved in the biosynthesis of two characteristic γ-glutamyl compounds occurring in Agaricus bisporus: agaritine and γ-glutaminyl-4-hydroxybenzene. Agaritine was shown to be a precursor of potential toxic aryl diazonium ions and γ-glutaminyl-4-hydroxybenzene was demonstrated to be one of the main substrates implicated in mushroom browning. γ-G;utamyl transferase activity was measured in various tissues of A. bisporus fruitbodies at different developmental stages and in mycelium grown on synthetic and compost media. Gills and skin, which exhibit the highest levels of γ-glutamyl amino acids, also present the highest levels of γ-glutamyl transferase activity. Stipe base tissue, which is characterised by a lack of agaritine and the presence of its hydrolysis product hydroxymethylphenylhydrazine, also exhibits high levels of γ-glutamyl transferase activity. Thus, in the gills and in the skin, γ-glutamyl transferase could be mainly involved in the synthesis of γ-glutamyl derivatives and, in the stipe base, in the hydrolysis of agaritine. γ-Glutamyl transferase activity measured in mycelia was rather low but significantly greater in mycelium grown on compost medium than on synthetic medium. These results are in agreement with the lack of γ-glutaminyl-4-hydroxybenzene in mycelium grown on artificial medium. Cap flesh and stipe tissues show the lowest γ-glutamyl transferase activity. The elucidation of the role of γ-glutamyl transferase in the synthesis of one of the main substrates for mushroom browning opens new perspectives in attempts to optimise post-harvest quality. |
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2 |
| title_short |
Space-time distribution of γ-glutamyl transferase activity in Agaricus bisporus |
| url |
http://dx.doi.org/10.1111/j.1574-6968.1998.tb13055.x |
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| author2 |
Mooibroek, Hans Wichers, Harry J. |
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| doi_str |
10.1111/j.1574-6968.1998.tb13055.x |
| up_date |
2024-07-06T03:38:37.770Z |
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