Relationships of Hydrophobicity to Emulsifying Properties of Heat Denatured Proteins

Abstract

Effects of heating on the emulsifying properties of selected food proteins and the protein surface hydrophobicity (So) as a predictor of these properties were investigated. The emulsifying properties of the proteins studied were differently affected by heating. Heatdenaturation was not always accompanied by loss of emulsifying properties, but, on the contrary, in some cases resulted in great improvement. The emulsifying properties could welI be predicted solely on the basis of So level but not on the basis of solubihty level, which indicated that So is a very important property determining protein functionality. However, the emulsifying activity, emulsion stability and fat binding capacity of the proteins studied could be explained and more accurately predicted using So and solubihty together.

Increased Antioxidative Activity of Ovalbumin by Heat Treating in an Emulsion of Linoleic Acid

“…These results agree with previous findings that both the hydrophobicity and emulsifying properties of ovalbumin could be markedly improved by heating. 18,20) Although native ovalbumin is the least hydrophobic protein,33) thermal denaturation makes this protein more amphiphilic by inducing unfolding of the molecule and exposing hydrophobic amino acid residues.…”

“…Ovalbumin (Grade V). polyoxyethylene (20) sorbitan monolaurate (Tween 20). nicotinamide adenine dinucleotide (NADH).…”

Improvement of gums in physicochemical and rheological properties of barley-fortified saltine cracker dough

“…Protein denaturation and unfolding facilitated the exposure of hydrophobic groups in gluten proteins and promote the hydrophobic interactions among them (Voutsinas et al 1983); as a result, the water absorption and gelatinization of starch granules were enhanced. Mixolab results showed that C3 and starch gelatinization rate (β) were reduced by the involved arabic gum, guar gum, or xanthan gum.…”

Comparison of emulsifying properties of milk fat globule membrane materials isolated from different dairy by-products

“…In addition, the BMP used in this study was heat treated during the previous production. Excessive heat denaturation may impair the emulsifying properties by rendering the protein insoluble (Voutsinas et al, 1983). With the same BMP concentration added, emulsion Lac40 contained more aggregates than emulsion BM-MFGM40.…”