Wheat proteins hydrophobic effect

EsterificaticMi with a fatty alcohol modified the functional properties of proteins, particularly their solubility in alkaline water. For wheat gluten and sunflower esterified proteins, solubility at basic pH decreased compared to native proteins, indicating thus a hydrophobation effect Fig 4 shows the effect of esterification on solubility of sunflower proteins. The solubility of unmodified sunflower proteins increased significantly in alkaline media and... 

PC loadings and their absolute values in the data reduction techniques has been proposed. This procedure has been successfully used for the smdy of the effect of carboxymethyl-P-cyclodextrin on the hydrophobicity parameters of steroidal drugs measured by TLC, and for the assessment of the binding characteristics of environmental pollutants to the wheat protein, gliadin, investigated by HPLC. 

The use of protein hydrolysates and quaternized derivatives in shampoo formulations has been demonstrated to reduce the loss of tensile strength caused by anionic tensides on the hair fibers (124,125). This protective effect is higher for quaternized derivatives than for parent hydrolysates. A wheat protein hydrolysate was found to be more effective than a collagen hydrolysate. Since the two tested products had similar isoelectric point and average molecular size, the difference could be explained by the higher hydrophobicity of the vegetable derivative. 

Proteins valorization as thermoplastic or thermosetting materials has been performed by chemical modifications [212]. Improved functional properties can be obtained by esterification of protein carboxyl and amide groups by fatty alcohol that lead to a protein-derivative with improved functional properties which would result into a lower water sensitivity. For example sunflower and wheat gluten have been esterified by octanol in the presence of an acid catalyst. Esterified protein result less soluble at basic pH compared to native proteins, indicating a hydrophobation effect [213]. 

Preston, K. R. 1981. Effects of neutral salts upon wheat gluten protein properties. I. Relationships between the hydrophobic properties of gluten proteins and their extractability and turbidity in neutral salts. Cereal Chemistry 58 317-324. 

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