Abstract
AbstractSoy proteins fractionated by the modified Nagano process (Nagano method) and a simplified pilot‐plant process (CCUR method) were studied for their functional properties, including solubility, viscosity, emulsification, and foaming. The functional properties of the three fractions produced by the Nagano method—glycinin (11S), β‐conglycinin (7S), and an intermediate fraction (IM)—were studied under a selected range of pH, ionic strengths, and protein concentrations. The 11S fraction was more soluble than the 7S at pH 2–3, whereas the 7S was more soluble than 11S at pH 5–6. Adding NaCl changed the solubility of both fractions at pH 4–5 compared to a neutral pH. Other functional properties were related to solubility in the 7S and 11S fractions. The CCUR method yielded only two fractions, 11S and 7S, and the functionality of those fractions was tested at a neutral pH. The solubility of the CCUR samples was slightly higher at extreme pH levels compared to 11S and 7S fractions from the Nagano method at a neutral pH. The relationship between solubility and other functional properties was clearer in CCUR samples. These results indicate that the simplified pilot‐scale CCUR fractionation process can influence the functional properties of the protein fractions.
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