Purification of catecholase from Solanum melangema (brinjal)

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dc.contributor.authorGoswami, Anita
dc.contributor.authorAmarapurkar, Sudha, V
dc.date.accessioned2011-11-30T07:09:58Z
dc.date.available2011-11-30T07:09:58Z
dc.date.issued2011-11
dc.description.abstractCatecholase was purified from cortex of Solanum melangena (brinjal) on natural affiant, lignin. The elution profile showed seven peaks withthe 6th peak having 4616-fold purity. The 6th pure fraction loaded on PAGE showed two protein bands on staining with Coomassie brilliant blue, one at the point of application and other neat he dye front. These bands exhibited catecholase activity, when stained with4-methyl catechol and proline, Basic fuschin and ethidium bromide showed positive tests, indicating that catecholase is a ribonucleoglycoprotein.en_US
dc.identifier.urihttp://dspace.vpmthane.org:8080/jspui/handle/123456789/2135
dc.subjectSolanumen_US
dc.subjectmelangenaen_US
dc.subjectpolyphenol oxidaseen_US
dc.subject4-methyl catecholaseen_US
dc.subjecto-diphenol oxidaseen_US
dc.subjectbrinjalen_US
dc.titlePurification of catecholase from Solanum melangema (brinjal)en_US
dc.typeArticleen_US
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Purification of catecholase from Solanum melangema (brinjal)