Isolation and in vitro hydrolysis of lentil protein fractions by trypsin / Aislamiento e hidrólisis \"in vitro\" de las fracciones proteínicas de la lenteja por la tripsina
Arch. latinoam. nutr
;
46(3): 238-42, sept. 1996. ilus, tab
Article
in Spanish
| LILACS
| ID: lil-217581
ABSTRACT
The albumin and globulin fractions from lentil seeds were isolated and characterised by gel filtration. The latter was shown to be homogeneous and the formet heterogeneous on PAGE, the aminoacid 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 30kD) 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 protein-protein interactions induced by heat
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Index:
LILACS (Americas)
Main subject:
In Vitro Techniques
/
Trypsin
/
Proteins
/
Hydrolysis
/
Fabaceae
Language:
Spanish
Journal:
Arch. latinoam. nutr
Journal subject:
Bioqu¡mica
/
EducaÆo Alimentar e Nutricional
/
Fenmenos Fisiol¢gicos da NutriÆo
/
Microbiologia de Alimentos
/
NUTRICAO
Year:
1996
Type:
Article
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