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Master's Dissertation
DOI
10.11606/D.9.1982.tde-01112012-105344
Document
Author
Full name
Adelaide Tie Catutani
E-mail
Institute/School/College
Knowledge Area
Date of Defense
Published
São Paulo, 1982
Supervisor
Title in Portuguese
Pectinesterase do mamão (Carica papaya L.)
Keywords in Portuguese
Ativação enzimática (Pesquisa - Características)
Bioquímica de alimentos
Carica papaya
Mamão
Pectinesterase
Propriedades bioquímicas
Proteínas (Estudo - Pesquisa)
Purificação enzimática
Abstract in Portuguese
Não consta resumo na publicação.
Title in English
Pectinesterase from papaya (Carica papaya L.)
Keywords in English
Biochemical properties
Carica papaya
Enzimatic activation
Enzimatic purification
Food biochemistry
Pectinesterase
Proteins
Abstract in English
Pectinesterase (E C 3.1.1.11) was extracted from papaya (Carica papaya L.) tissue and purified 4,48 fold by fractionated ammonium sulphate precipitation, dialysis and chromatography on DEAE-celulose and Sephadex G-100. Extraction conditions of enzyme were studied and their properties characterized. The increase on the activity of pectinesterase was practically followed by increase on the content of soluble pectin, during ripening. The molecular weight of the enzyme eluted in one peak of activity was 53.000 daltons. The pectinesterase has its maximum activity at pH 8,0 and at 0,2 M of NaCl. Optimum temperature for the enzyme assay was 60°C. The enzymatic reaction was linear with the time and protein concentration. With citric pectin as substrate, pectinesterase had a Km of 0,012% and was inhibited competitively by polygalacturonic acid with a Ki of 0,007%. Papaya pectinesterase was inhibited by sucrose, glucose and glicerol.
 
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Publishing Date
2012-11-01
 
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