Denaturation and enzymatic proteolysis in vitro of protein fractions of soya flour

• Published in: Annales de la nutrition et de l'alimentation 1975, Vol.29 (4), p.351-370
• Main Authors: Bau, H M, Alais, C
• Format: Article
• Language: fre
• Subjects: Ethanol; Flour; Glycine max - analysis; Hot Temperature; Pepsin A - metabolism; Plant Proteins, Dietary - isolation & purification; Plant Proteins, Dietary - metabolism; Protein Denaturation; Solubility; Trypsin - metabolism
• ISSN: 0003-4037

Soya, in spite of its high nutritional value and moderate cost, possesses certain undesirable qualities which limit its use in animal and human nutrition. The amendment of these qualities has resulted in much work. In this study the effects of technological treatments on the properties of certain protein fractions capable of being produced industrially were observed. Three fractions were prepared from defatted soybean flour of the "Harosoy 63" variety: an acid-precipitated fraction, a cold-insoluble fraction at 0-3 degrees C, and a water-soluble fraction. The properties of the fractions were studied both before denaturation and after denaturation by either heat or alcohol. The degree of proteolysis of each fraction by two digestive enzymes, pepsin and trypsin, was measured by the increase of non-protein nitrogen as a function of time. Several methods were used for electrophoretic analysis. The results showed that the thermal treatment at 100 degrees C and the treatment with varying concentrations of ethanol (from 10 to 100 p. 100) modified electrophoretic diagrams and the solubility of the proteins in trichloracetic acid. Moderate, moist heating of the protein fractions (100 degrees C, 20 mn) before proteolysis by pepsin and trypsin, in general, favored proteolysis. The most marked effect observed was in the acid-precipitated fraction (in which Kunitz inhibitor was concentrated treated by trypsin. Heating the fractions beyond thirty minutes had a negative effect on proteolysis: the level of proteolysis was the same, or in some cases, lower than before denaturation, especially on subsequent treatment with pepsin. The effects of the ethanol treatment were different from that of heat: the proteolysis was accelerated only with the acid-precipitated fraction.