RESUMO
The chickpea seed germination was carried out in 6 days. During the period it was observed a little variation on total nitrogen contents, however the non protein nitrogen was double. A decrease of 19.1 and 20.6% in relation to total nitrogen was observed to the total globulin and albumin fractions, respectively. The gel filtration chromatography on Sepharose CL-6B and SDS-PAGE demonstrated alterations on the distribution patterns of the albumin and total globulin fractions between the initial and the sixth day of germination suggesting the occurrence of protein degradation in the germination process. The assay for acid protease only appeared in the albumin fraction with casein and chickpea total globulin as substrates, whereas the former was more degraded than the latter, however the transformations detected in the protein fractions appear indicated that others enzymes could be acting during the process. The trypsin inhibitor activity had a little drop after six day of germination indicating a possible increase on the digestibility of the proteins.
Assuntos
Cicer/metabolismo , Cotilédone/metabolismo , Germinação , Peptídeo Hidrolases/metabolismo , Proteínas de Plantas/metabolismo , Inibidores da Tripsina/metabolismo , Albuminas/química , Albuminas/metabolismo , Cromatografia em Gel , Cicer/enzimologia , Cicer/crescimento & desenvolvimento , Cotilédone/enzimologia , Eletroforese em Gel de Poliacrilamida , Globulinas/química , Globulinas/metabolismo , Nitrogênio/metabolismo , Proteínas de Plantas/química , Sementes/metabolismo , Sefarose/químicaRESUMO
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.