Journal
FOOD CHEMISTRY
Volume 210, Issue -, Pages 520-529Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2016.04.113
Keywords
Wheat gluten; Deamidation; Aggregation; Functional properties; Structure; Processing conditions
Funding
- National Natural Science Foundation of China [31201287]
- Natural Science Foundation of Fujian Province of China [2015J05067]
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The physicochemical, structural and functional properties of citric-acid-deamidated wheat gluten at controlled degrees of deamidation (25%, 40% and 55%), which were obtained by using different acid concentrations (3.93 x 10(-5), 3.14 x 10(-3) and 2.36 x 10(-2) mol/L) and temperatures (70 degrees C 2 h, 90 degrees C 1h and 110 degrees C 40 min), were compared. Various deamidation processing conditions leading to the same degree of deamidation resulted in proteins with different physicochemical and structural characteristics, as indicted by the degree of hydrolysis, Z-potential, surface hydrophobicity, particle size, SDS-PAGE results, SEC-HPLC results, intrinsic fluorescence and FTIR spectra. Agglomerative hierarchical clustering analysis and principal component analysis qualitatively indicated a significant effect of pH on protein deamidation. Three samples at 40% deamidation, which were produced by a moderate acid concentration, showed the best emulsifying and foaming properties. Processes conducted at greater than 90 degrees C causing protein aggregation and at a high acid concentration rupturing peptide bonds, impaired protein quality. These findings demonstrated that a limited amount of H+ could function well in the catalysis of the deamidation of amide groups without an excess of H+, which hydrolyses peptide bonds in a stronger hydrothermal treatment. (C) 2016 Elsevier Ltd. All rights reserved.
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