Physicochemical properties of alkali-treated oat globulin
1990
Ma, C.Y. | Harwalkar, V.R. | Paquet, A.
Oat globulin dispersions (10% w/v) were incubated at an initial pH of 9.8 at 25, 37, and 55 degrees C over a period of 96 h. Turbidity increased at 25 and 37 degrees C with the formation of insoluble aggregates and decreased at 55 degrees C with little precipitation. The free SH content decreased progressively with time, while the surface hydrophobicity was increased at 25 degrees C and decreased at 37 degrees C. Differential scanning calorimetry showed progressive increases in denaturation temperature and decreases in width at half-peak height. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated formation of soluble aggregates at 55 degrees C and degradation of oat globulin polypeptides at 25 and 37 degrees C, possibly due to proteolysis by protease(s) coextracted with the protein. No significant racemization of amino acids was observed in the alkali-treated protein.
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