Surface and interfacial properties of water-soluble wheat proteins
- 作者：K. Hill ; E. Horvá ; th-Szanics ; Gy. Hajó ; s ; É ; . Kiss
- 关键词：Adsorption of wheat proteins ; Preparative isoelectric focusing ; Surface/interfacial tension ; Dilatational rheology ; Interfacial elastic modulus
- 刊名：Colloids and Surfaces A ; Physicochemical and Engineering Aspects
- 出版年：2008
- 期刊代码：22_09277757
- 类别：ch
- 出版时间：15 April 2008
- 卷：319
- 期：1-3
- 页码：180-187
- 文件大小：846 K
摘要
Surface and interfacial properties of water-soluble wheat proteins were investigated and compared with six reference proteins (bovine serum albumin, ovalbumin, β-lactoglobulin, trypsin, cytochrom C and β-amylase). Albumins extracted from wheat flour were separated by the free solution isoelectric focusing. The surface activity at the air/water, dodecane/water interfaces and dilatational rheological behaviour of the adsorbed layers was determined by pendant drop technique. Considerably high surface activity of wheat proteins was found at both interfaces exceeding the corresponding values of most of the reference proteins. Exceptionally, low dilatational moduli (typically 
< 10 mN/m) were obtained for wheat fractions in the continuous and the stepwise compression experiments with no age effect (1–20 min) and almost no relaxation. Surface/interfacial activity and rheological properties observed imply that water-soluble wheat proteins are generally characterized by strong hydrophobicity and more flexible molecular structure than the reference proteins.
< 10 mN/m) were obtained for wheat fractions in the continuous and the stepwise compression experiments with no age effect (1–20 min) and almost no relaxation. Surface/interfacial activity and rheological properties observed imply that water-soluble wheat proteins are generally characterized by strong hydrophobicity and more flexible molecular structure than the reference proteins.