Partial purification and characterization of polyphenoloxidase from peppermint (Mentha piperita)

dc.contributor.authorKavrayan, D
dc.contributor.authorAydemir, T
dc.date.accessioned2024-07-18T11:46:39Z
dc.date.available2024-07-18T11:46:39Z
dc.description.abstractPolyphenoloxidase (PPO) of peppermint leaves (Mentha piperita) was isolated by (NH4)(2)SO4 precipitation and dialysis. Its pH and temperature optima were 7.0 and 30 degreesC, respectively. On heat-inactivation, half of the activity was lost after 6.5 and 1.5 min of treatment at 70 and 80 degreesC, respectively. Sucrose, (NH4)(2)SO4, NaCl and KCl appeared to be protective agents of peppermint PPO against thermal denaturation. Km of this enzyme ranged from 6.25 x 10(-3) M with catechol to 9.00 x 10(-3) M with L-dopa. The I-50 values of inhibitors studied on PPO were determined by means of activity percentage (I) diagrams. Values were 1.4 x 10(-4) M, 1.7 x 10(-4) M, 9.7 x 10(-5) M, 2.45 x 10(-4) M, 2.16 x 10(-1) M, 1.83 x 10(-5) M, 6.5 x 10(-5) M, 1.4x 10(-2) M, 7.5 x 10(-5) M, for potassium cyanide, glutathione, ascorbic acid, thiourea, sodium azide, sodium metabisulfite, dithioerythritol, beta -mercaptoethanol and sodium diethyl dithiocarbamate respectively, Therefore, sodium metabisulfite was the most effective inhibitor. (C) 2001 Elsevier Science Ltd. All rights reserved.
dc.identifier.issn0308-8146
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/2901
dc.language.isoEnglish
dc.publisherELSEVIER SCI LTD
dc.subjectINDUCED REVERSIBLE DENATURATION
dc.subjectPYRUS-COMMUNIS L
dc.subjectMONOHYDRIC ALCOHOLS
dc.subjectOXIDASE
dc.subjectPROTEINS
dc.subjectPEARS
dc.subjectPRECIPITATION
dc.subjectVARIETY
dc.subjectPLANTS
dc.subjectGRAPES
dc.titlePartial purification and characterization of polyphenoloxidase from peppermint (Mentha piperita)
dc.typeArticle

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