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  • Exploring the Relationship between Structural and Air-Water Interfacial Properties of Wheat (Triticum aestivum L.) Gluten Hydrolysates in a Food System Relevant pH Range.

Exploring the Relationship between Structural and Air-Water Interfacial Properties of Wheat (Triticum aestivum L.) Gluten Hydrolysates in a Food System Relevant pH Range.

Journal of agricultural and food chemistry (2017-01-27)
Arno G B Wouters, Ellen Fierens, Ine Rombouts, Kristof Brijs, Iris J Joye, Jan A Delcour
ABSTRACT

The relationship between structural and foaming properties of two tryptic and two peptic wheat gluten hydrolysates was studied at different pH conditions. The impact of pH on foam stability (FS) of the samples heavily depended on the peptidase used and the degree of hydrolysis reached. Surface dilatational moduli were in most, but not all, instances related to FS, implying that, although the formation of a viscoelastic protein hydrolysate film is certainly important, this is not the only phenomenon that determines FS. In contrast to what might be expected, surface charge was not a major factor contributing to FS, except when close to the point-of-zero-charge. Surface hydrophobicity and intrinsic fluorescence measurements suggested that changes in protein conformation take place when the pH is varied, which can in turn influence foaming. Finally, hydrolyzed gluten proteins formed relatively large particles, suggesting that protein hydrolysate aggregation probably influences its foaming properties.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Pepsin from porcine gastric mucosa, lyophilized powder, ≥3,200 units/mg protein
Sigma-Aldrich
Trypsin from porcine pancreas, Type IX-S, lyophilized powder, 13,000-20,000 BAEE units/mg protein