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  • Author or Editor: L. Jędrychowski x
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The possibilities of lowering the immunoreactive properties of hydrolysed pea globulins were examined in the presented work. The hydrolytic process with Alcalase, pepsin and trypsin was carried out at temperatures of 37 °C and 50 °C for 180 min. The highest degree of hydrolysis was obtained during hydrolysis with Alcalase (DH 25% at temperature of 50 °C). The highest reduction of immunoreactive properties of legumin and vicilin was observed after hydrolysis with trypsin (DH 12%) at 50 °C by 98% and 97.4%, respectively. Generally, the immunoreactivity of vicilin was reduced to a smaller extent than immunoreactivity of legumin during the hydrolysis processes analysed.

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Proteins of pea variety Kwestor, grown in Poland, were modified with acetic or succinic anhydride (0.01–1.0 g/g anhydride/protein). Degree of acylation, electrophoretic properties (SDS-PAGE) and immunoreactivity (by ELISA) were studied. The study indicates that not only the degree of acylation but also the type of anhydrides affected the extent of changes in the immunoreactivity of individual pea proteins. The greatest reductions in the immunoreactivity of albumins and legumin were observed during acylation with 0.2 g anhydrides (by 91–99% and 79–97% during succinylation and acetylation, respectively). The lowest immunoreactivity of vicilin fraction was found when 1.0 g of anhydride was used (about 6% during succinylation and 14.7% during acetylation as compared to the immunoreactivity of vicilin in native pea proteins).

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Commercial sodium caseinate isolate (SCI) was hydrolysed with either protease Subtilisina carlsberg - Alcalase 2.4 FG (purchased from Novo Nordisk), pronase from Streptomyces griseus, and papain EC 3.4.22.2 (both from Sigma) in a two-step process to determine the changes in the immunoreactivity of a-, ß- and ?-casein. Enzymatic hydrolysis of SCI was performed by pH-stat method. Hydrolysates were analysed using IEF, SDS-PAGE, 2D electrophoresis, FPLC-gel permeation chromatography. Immunoreactive properties of peptide fractions separated from the hydrolysates by FPLC were determined using dot-immunobinding and ELISA methods. The two-step process was observed to be effective in reduction of casein fractions immunoreactivity, however, allergenic epitopes were still present in all peptide fractions.

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In recent years, research related to studying the effect of gut microflora on the human health has become of major economic importance. The main objective of our study was to examine whether or not the orally administered Lactobacillusstrains (LB) as an oral adjuvant can improve the mucosal immune protectionviaan enhanced IgA secretion to a co-administered marker antigen ovalbumin (OVA). We adapted a murine (BALB/c) model to demonstrate beneficial adjuvant effects of probiotic LB strains. Orally sensitised mice with OVA, which were prefed with native or heat denatured (HD) Lactobacillus salivarius (Ls) or Lactobacillus casei (Lc) responded better or with the same efficiency to a vaccination with antigen (OVA) than mice that had been sensitised only with OVA or not sensitised at all. Antibody (IgA) responses in the gut were increased in response to vaccination with OVA in mice that had been prefed with native or heat denatured Ls or Lc followed by Ls or Lc and OVA feeding. In prefed groups, the OVA feeding alone primed for specific immune response, while adjuvanted OVA has increased the immune exclusion potential of the gut.

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