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Aggregation characteristics of protein during wheat flour maturation
Author(s) -
Wang Na,
Ma Sen,
Li Li,
Zheng Xueling
Publication year - 2018
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.9239
Subject(s) - glutenin , gluten , food science , chemistry , gliadin , disulfide bond , random coil , high protein , wheat flour , protein aggregation , wheat gluten , protein quality , particle size , biochemistry , protein secondary structure , protein subunit , gene
BACKGROUND The protein aggregation characteristics of three types of freshly milled wheat flour with high, medium or low gluten were investigated during 90 days of maturation. Changes in the content and particle size of the glutenin macropolymer (GMP), contents of sulfhydryl groups and disulfide bonds (SS), and secondary structure and molecular weight distribution of the protein were determined. RESULTS For high, medium and low gluten flour, GMP content increased to 22.25, 13.72 and 10.32 g kg −1 ; free sulfhydryl group content decreased by 5.5%, 4.1% and 4.4%; and SS content increased by 1.6%, 1.8% and 2%, respectively. The proportion of β ‐sheet and random coil increased, and the proportion of α ‐helix and β ‐turns decreased. The polymeric protein content increased, whereas that of gliadin decreased. CONCLUSION Protein aggregation mediated by SS cross‐linking helped develop a stronger gluten network. The findings provide theoretical support for the changes in protein structure during flour maturation and also help to predict the quality of wheat flour and its products. © 2018 Society of Chemical Industry