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Hydrolysis of soybean isoflavones by Debaryomyces hansenii UFV-1 immobilised cells and free ß-glucosidase.
Maitan-Alfenas, Gabriela P; de A Lage, Lorena G; de Almeida, Maíra N; Visser, Evan M; de Rezende, Sebastião T; Guimarães, Valéria M.
Afiliação
  • Maitan-Alfenas GP; Dep. Bioquímica e Biologia Molecular, BIOAGRO, Universidade Federal de Viçosa, Viçosa, MG 36.570-000, Brazil.
Food Chem ; 146: 429-36, 2014 Mar 01.
Article em En | MEDLINE | ID: mdl-24176363
An intracellular ß-glucosidase from Debaryomyceshansenii UFV-1 was produced in an YP medium with cellobiose as the carbon source. This enzyme was purified, characterised and presented a Mr of 65.15kDa. Yeast cells containing the intracellular ß-glucosidase were immobilised in calcium alginate. The free ß-glucosidase and immobilised cells containing the enzyme presented optima values of pH and temperature of 6.0 and 45°C and 5.5 and 50°C, respectively. The free enzyme maintained 62% and 47% of its original activity after 90days at 4°C and after 15days at room temperature, respectively. The immobilisation process resulted in higher enzyme thermostability at 45 and 50°C. Soy molasses treatment with the free enzyme and the immobilised cells containing ß-glucosidase, for 2h at 40°C, promoted efficient hydrolysis of isoflavone glicosides to their aglycon forms. The results suggest that this enzyme could be used in the food industry, in the free or immobilised forms, for a safe and efficient process to hydrolyse isoflavone glycosides in soy molasses.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glycine max / Proteínas Fúngicas / Beta-Glucosidase / Debaryomyces / Isoflavonas Idioma: En Revista: Food Chem Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Brasil País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glycine max / Proteínas Fúngicas / Beta-Glucosidase / Debaryomyces / Isoflavonas Idioma: En Revista: Food Chem Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Brasil País de publicação: Reino Unido