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Changes in
protein fractions, trypsin inhibitor and proteolytic activity in the cotyledons
of germinating chickpea.
Arch Latinoam Nutr 2001 Sep;51(3):269-75
Neves VA, Lourenco EJ.
Universidade Paulista Julio de Mesquita Filho-UNESP, Sao Paulo, Brasil.
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.
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