alpha-chymotrypsin and kaempferol

Soy glycinin (SG) and soy trypsin inhibitor (STI) were derivatized by chlorogenic- and caffeic acid (cinnamic acids, C(6)-C(3) structure), and by gallic acid representing hydroxybenzoic acids (C(6)-C(1) structure). Further, the flavonoids, flavone, apigenin, kaempferol, quercetin and myricetin (C(6)-C(3)-C(6) structure) were also caused to react with soy proteins to estimate the influence of the number and the position of hydroxy substituents. The derivatization caused a reduction of lysine, cysteine and tryptophan residues in the soy proteins. The isoelectric points of the derivatives were shifted to lower pH values and formation of high molecular fractions was documented. The derivatives were characterized in terms of their solubility at different pH-values to document the influence on the functional properties. The structural changes induced were studied using circular dichroism (CD), differential scanning calorimetry (DSC), intrinsic fluorescence, and binding of anilinonaphthalenesulfonic acid. The influence of derivatization on the in-vitro digestibility with trypsin, chymotrypsin, pepsin and pancreatin was also assessed. The effect on the trypsin inhibitor activity of all the resulting STI derivatives was studied, the latter being reduced.

Topics: Anilino Naphthalenesulfonates; Apigenin; Calorimetry, Differential Scanning; Caseins; Chymotrypsin; Circular Dichroism; Flavones; Flavonoids; Fluorescence; Globulins; Hydroxybenzoates; Kaempferols; Pancreatin; Pepsin A; Quercetin; Soybean Proteins; Structure-Activity Relationship; Trypsin; Trypsin Inhibitor, Kunitz Soybean