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Type: Artigo de periódico
Title: Enzyme Characterisation, Isolation And Cdna Cloning Of Polyphenol Oxidase In The Hearts Of Palm Of Three Commercially Important Species.
Author: Shimizu, Milton Massao
Melo, Geraldo Aclécio
Brombini Dos Santos, Adriana
Bottcher, Alexandra
Cesarino, Igor
Araújo, Pedro
Magalhães Silva Moura, Jullyana Cristina
Mazzafera, Paulo
Abstract: Heart of palm (palmito) is the edible part of the apical meristem of palms and is considered a gourmet vegetable. Palmitos from the palms Euterpe edulis (Juçara) and Euterpe oleracea (Açaí) oxidise after harvesting, whereas almost no oxidation is observed in palmitos from Bactris gasipaes (Pupunha). Previous investigations showed that oxidation in Juçara and Açaí was mainly attributable to polyphenol oxidase (PPO; EC activity. In this study, we partially purified PPOs from these three palmitos and analysed them for SDS activation, substrate specificity, inhibition by specific inhibitors, thermal stability, optimum pH and temperature conditions, Km and Ki. In addition, the total phenolic content and chlorogenic acid content were determined. Two partial cDNA sequences were isolated and sequenced from Açaí (EoPPO1) and Juçara (EePPO1). Semi-quantitative RT-PCR expression assays showed that Açaí and Juçara PPOs were strongly expressed in palmitos and weakly expressed in leaves. No amplification was observed for Pupunha samples. The lack of oxidation in the palmito Pupunha might be explained by the low PPO expression, low enzyme activity or the phenolic profile, particularly the low content of chlorogenic acid.
Subject: Arecaceae
Catechol Oxidase
Cloning, Molecular
Dna, Complementary
Enzyme Inhibitors
Enzyme Stability
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Plant
Hydrogen-ion Concentration
Plant Proteins
Substrate Specificity
Citation: Plant Physiology And Biochemistry : Ppb / Société Française De Physiologie Végétale. v. 49, n. 9, p. 970-7, 2011-Sep.
Rights: fechado
Identifier DOI: 10.1016/j.plaphy.2011.04.006
Date Issue: 2011
Appears in Collections:Unicamp - Artigos e Outros Documentos

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