Binding of Alcohols by Soy Protein in Aqueous Solutions

Abstract

Interactions of alcohols with soy protein isolate were investigated using an equilibrium dialysis method. It was found that interactions may involve hydrophobic association and, to some degree, hydrogen bonding. Studies with soy protein with various levels of denaturation indicated that denaturation of the protein by heating may limit its ability for the formation of hydrogen bonds with alcohols. The proteins under investigation exhibited practically unlimited binding capacity for alcohols.

Coating papers with soy protein isolates as inclusion matrix of carvacrol

“…Therefore, the thermodynamic affinity between protein molecules and aroma compounds increased in the case of the native protein and was reduced with heat-denatured protein. These observations agree with the findings reported by Chung and Villota (1989) that the association of alcohol is weaker when soy proteins are denatured. 8.9 ± 0.7 2.9 ± 0.2 1.8 ± 0.2 37.9 ± 5.3 66.0 ± 6.0 a Carvacrol losses were determinated from quantity of carvacrol extracted at 50 days from papers related to the quantity extracted from the coated papers after coating and drying process.…”

Competitive Binding of Off‐Flavor Compounds with Soy Protein and β‐Cyclodextrin in a Ternary System: A Model Study

“…[1][2][3][4][5][6]. Once formed, these volatile compounds bind to SP via non-covalent interactions [7][8][9][10][11][12][13]. Common processing methods employed for the isolation of SP from soybean are often inadequate to overcome this binding.…”

Effect of feed pH and non-volatile dairy components on flavour concentration by pervaporation

“…Soy proteins are known to bind alcohols (Chung and Villota, 1989), but it is unlikely that this level of protein bound enough of the 2% ethanol to see a significant effect. Assuming a molecular weight of at least 150,000 g mol À1 for soy protein (Fukushima, 2004), Aroujalian et al's (2003) feed solution contained 7 Â 10 À5 mol L À1 protein and 0.43 mol L À1 ethanol.…”