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Substrate Specificity, Heat Inactivation and Inhibition of Polyphenoloxidase From Anethum Graveolens L

dc.authorscopusid 35974671200
dc.authorscopusid 6507332990
dc.contributor.author Arslan, O
dc.contributor.author Tozlu, I
dc.date.accessioned 2025-05-10T16:58:42Z
dc.date.available 2025-05-10T16:58:42Z
dc.date.issued 1997
dc.department T.C. Van Yüzüncü Yıl Üniversitesi en_US
dc.department-temp Yuzuncu Yil Univ,Dept Chem,Van,Turkey en_US
dc.description.abstract Polyphenoloxidase (PPO), isolated from Anethum graveolens L, showed activity on catechol, L-tyrosine and DL-DOPA. The optimum pH for the PPO was 7.0. Heat inactivation studies showed that heating for 40 and 15 min at 60 degrees and 80 degrees C, respectively, caused a 50% loss in enzymatic activity. The enzyme catalysed browning reaction was significantly inhibited in the presence of ascorbic acid, 2-mercaptoethanol, uric acid and barbituric acid. The most effective inhibitors were ascorbic acid and 2-mercaptoethanol. en_US
dc.description.woscitationindex Science Citation Index Expanded
dc.identifier.endpage 253 en_US
dc.identifier.issn 1120-1770
dc.identifier.issue 3 en_US
dc.identifier.scopus 2-s2.0-0031493347
dc.identifier.scopusquality Q2
dc.identifier.startpage 249 en_US
dc.identifier.uri https://hdl.handle.net/20.500.14720/4352
dc.identifier.volume 9 en_US
dc.identifier.wos WOS:A1997YA11800009
dc.identifier.wosquality Q3
dc.language.iso en en_US
dc.publisher Chiriotti Editori en_US
dc.relation.publicationcategory Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı en_US
dc.rights info:eu-repo/semantics/closedAccess en_US
dc.subject Anethum Graveolens L. en_US
dc.subject Herbal Cheese en_US
dc.subject Inhibition en_US
dc.subject Polyphenoloxidase en_US
dc.title Substrate Specificity, Heat Inactivation and Inhibition of Polyphenoloxidase From Anethum Graveolens L en_US
dc.type Article en_US

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