Acta Alimentaria · 2005 · 12 citations · 21 references
Life SciencesBiochemistryPlant BiologyEnzymologyPlant BiochemistryProtein BiochemistryGlycan AnalysisGlycan DegradationProtein AnalysisProteins In FoodsProteolytic EnzymesEnzymatic Hydrolysis Of ProteinsPlant ProteasesProteolytic Activity
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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