Isolation and in vitro hydrolysis of lentil protein fractions by trypsin.
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.
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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