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Isolation and in vitro hydrolysis of lentil protein fractions by trypsin.
Neves, V A; Lourenço, E J; da Silva, M A.
Afiliação
  • Neves VA; Departamento de Alimentos e Nutrição Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista UNESP-Araraquara, S. Paulo, Brasil.
Arch Latinoam Nutr ; 46(3): 238-42, 1996 Sep.
Article em En | MEDLINE | ID: mdl-9429629
The albumin and globulin fractions from lentil seeds were isolated and characterised by gel filtration. The latter was shown to be homogeneous and the former heterogeneous on PAGE. The amino acid analysis revealed high values of amidic amino acids for both fractions with great differences in the sulphur-containing amino acids. Native albumin, globulin and salt-soluble proteins were markedly resistant to trypsin hydrolysis compared to casein. The SDS-PAGE of native salt-soluble proteins indicated that the globulin fragments (20 to 30 kD) were slowly digested in the presence of albumin. The heating increased the hydrolysis of the proteins in the order: salt-soluble, albumin and globulin. The facilitated hydrolysis of the heated salt-soluble fraction seemed to be due to protein-protein interactions induced by heat.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Plantas Medicinais / Tripsina / Fabaceae Idioma: En Revista: Arch Latinoam Nutr Ano de publicação: 1996 Tipo de documento: Article País de afiliação: Brasil País de publicação: Venezuela
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Plantas Medicinais / Tripsina / Fabaceae Idioma: En Revista: Arch Latinoam Nutr Ano de publicação: 1996 Tipo de documento: Article País de afiliação: Brasil País de publicação: Venezuela