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LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
Published on: April 9, 2017
Comparative characterization of the deamidation of carboxylic acid deamidated wheat gluten by altering the processing
Lan Liao1, Xueyue Han1, Lin-Ping Chen1
1Institute of Food Science and Technology, College of Biological Science and Technology, Fuzhou University, Fuzhou, Fujian 350108, People's Republic of China; Fujian Center of Excellence for Food Biotechnology, Fuzhou University, Fuzhou, Fujian 350108, People's Republic of China.
Abstract:
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 (3.93×10(-5), 3.14×10(-3) and 2.36×10(-2)mol/L) and temperatures (70°C 2h, 90°C 1h and 110°C 40min), 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°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.
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