Record Details


Field	Value

Title	Characterization of tyrosinase and accompanying laccase from Amorphophallus campanulatus

Creator	Paranjpe, Pallavi S Karve, Meena S Padhye, Subhash B

Description	40-45 Tyrosinase and laccase activities were detected in the corm of Amorphophallus campanulatus after extraction with ethanol followed by ammonium sulphate precipitation (20-60%) and dialysis against 10 mM Na₂HPO₄ buffer at pH 7.0. Tyrosinase was found to be the predominant enzyme exhibiting mono- and di-phenolase activities, specificity for L-DOPA as substrate, optimum pH being 6.0, optimum temperature at 40ºC and Km at 1.05 mM. Laccase showed substrate specificity for p-phenylenediamine (p-PD), Km at 2.7 mM, optimum pH being 5.0 and was inactivated above 40ºC. Three isoforms of tyrosinase were detected on SDS-PAGE with apparent molecular mass ~127, 31 and 27 kDa respectively. On staining sections of A. campanulatus with L-DOPA as substrate and 3-methyl benzothiazolinone hydrazone (MBTH) for colour development, tyrosinase was detected in the intercellular spaces of the plant tissue. The cytosolic region did not show any colour indicating the absence of the enzyme.

Date	2009-04-06T09:26:30Z 2009-04-06T09:26:30Z 2003-02

Type	Article

Identifier	0301-1208 http://hdl.handle.net/123456789/3738

Language	en_US

Publisher	CSIR

Source	IJBB Vol.40(1) [February 2003]

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