Search Results

You are looking at 1 - 2 of 2 items for :

  • Author or Editor: György Hajós x
  • Biology and Life Sciences x
  • Refine by Access: All Content x
Clear All Modify Search

Buffalo and cow milk caseins were submitted to hydrolysis either with á -chymotrypsin or with pepsin. Enzymatic peptide modification (EPM) was carried out by using L-methionine ethyl ester in the reaction mixture. As catalyst, á -chymotrypsin or pepsin was used. The incorporation of methionine in to the peptide chains in the presence of á -chymotrypsin showed an optimum value at 0.14 g Met added to the reaction mixture/1 g hydrolysate in both cases. In the case of pepsin used as catalyst, the optimal Met-enrichment was at 0.14 g Met added to the reaction mixture/1 g buffalo casein hydrolysate and at 0.34 g Met/1 g cow casein hydrolysate. The covalent nature of the amino acid incorporation was confirmed by SDS - polyacryl amide gel electrophoresis in the presence of urea. Electrophoretic patterns of the products indicate that transpeptidation plays an essential role in the EPM reaction. Antigenic character of the EPM- products was investigated in vitro by competitive indirect ELISA. Enzymatic peptide modification with methionine enrichment seems to be an efficient method for the reduction of the antigenic/potential allergenic character and for the improvement of the nutritive value of buffalo and cow milk caseins.

Restricted access
Acta Alimentaria
C. Cuadrado
É. Gelencsér
M. M. Perdosa
G. Ayet
M. Muzquiz
A. Puszati
György Hajós
, and
C. Burbano

The effect of germination conditions on the lectin of Lens culinaris var. Magda 20 seeds was studied. The seeds were germinated at 20 °C under different conditions of watering and light and for different periods of time. The seed lectin was assayed by haemagglutination and quantified by competitive ELISA. Changes in lectin content during germination were also monitored by SDS-PAGE and immunoblotting. Haemagglutinating activity and lectin content in the seeds were not changed during the first three days regardless of the conditions of the germination. However, lectin concentration was significantly higher after six days of germination; relative lectin levels being particularly high when germination was carried out in the light and with daily watering. The results of SDS-PAGE and immunoblotting have also shown that the lectin was not degraded during the first six days of germination however, other storage-proteins were broken down by proteolysis.

Restricted access