Changes in the structural and physicochemical properties of wheat gliadin and maize amylopectin conjugates induced by dry-heating.

Abstract

The Maillard reaction (MR) has been known to modify proteins and optimize their physicochemical properties by conjugating with reducing sugars. The structure and physicochemical properties of wheat gliadin and maize amylopectin conjugates induced by MR were investigated under different gliadin-amylopectin ratios (2:1, 1:1, 1:2, 1:4, and 1:8). The formation of conjugates was indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, degree of conjugation, and browning development analyses. The Fourier transform infrared and fluorescence spectroscopy analyses suggested changes in the structures of conjugates and the microenvironment of amino acids. A remarkable decrease in the β-turn structure content and an increase in the free sulfhydryl group content were observed at a ratio of 1:8, leading to decreased allergenicity. The reaction process was commendably controlled at a ratio of 1:1 with a 59.7% degree of conjugation in this group, contributing to the amelioration of solubility and foaming properties. Meanwhile, improvements in the oil holding capacity, surface hydrophobicity, and emulsifying properties were observed at a ratio of 1:4. PRACTICAL APPLICATION: The study revealed that the conjugates produced by MR might have various degrees of improved functional properties and reduced allergenicity at different ratios of substrates. Our study might be helpful for conjugates to assist in improving the texture of products and its potential in expanding the industrial application of products with gliadin.