title: Effects of inulin on the structure and emulsifying properties of protein components in dough.
abstract: High-purity gliadin, glutenin and gluten fractions were extracted from wheat gluten flour. To investigate the effects of three types of inulin with different degrees of polymerization (DP) on the emulsifying properties, disulfide contents, secondary structures and microstructures of these fractions, Turbidimetry, spectrophotometer, Fourier transform infrared spectroscopy (FT-IR) and scanning electron microscopy (SEM) were used in this study. The results showed that the emulsifying activity of gliadin was higher than that of glutenin and gluten, but its emulsion stability was lower than that of glutenin. Adding inulin increased the emulsifying activity of the three protein fractions and emulsion stability of gliadin and gluten, but decreased the emulsion stability of glutenin and disulfide bond contents of glutenin and gluten. In the presence of inulin, the α-helical structure of the three proteins had no significant change, whereas the β-turn structure decreased and β-sheet structure increased. The SEM images showed that inulin had the most significant effect on the glutenin microstructure. In general, inulin with a higher DP had greater effects on the structure and emulsifying properties of protein components in dough.
authors.affiliation: College of Food and Bioengineering, Henan University of Science & Technology, 471023 Luoyang, Henan Province, China. Electronic address: 15236197261@163.com.
authors.forename: Juan
authors.initials: J
authors.lastname: Liu
authors.affiliation: College of Food and Bioengineering, Henan University of Science & Technology, 471023 Luoyang, Henan Province, China. Electronic address: luodenglin@163.com.
authors.forename: Denglin
authors.initials: D
authors.lastname: Luo
authors.affiliation: College of Food and Bioengineering, Henan University of Science & Technology, 471023 Luoyang, Henan Province, China.
authors.forename: Xuan
authors.initials: X
authors.lastname: Li
authors.affiliation: College of Food and Bioengineering, Henan University of Science & Technology, 471023 Luoyang, Henan Province, China.
authors.forename: Baocheng
authors.initials: B
authors.lastname: Xu
authors.affiliation: College of Food and Bioengineering, Henan University of Science & Technology, 471023 Luoyang, Henan Province, China.
authors.forename: Xiaoyu
authors.initials: X
authors.lastname: Zhang
authors.affiliation: College of Food and Bioengineering, Henan University of Science & Technology, 471023 Luoyang, Henan Province, China.
authors.forename: Jianxue
authors.initials: J
authors.lastname: Liu
mesh_terms: D004655:Emulsions / Q000737:chemistry*; D005433:Flour / Q000032:analysis*; D005903:Gliadin / Q000032:analysis; D005983:Glutens / Q000032:analysis; D007444:Inulin / Q000494:pharmacology; D058105:Polymerization / Q000187:drug effects; D011487:Protein Conformation / Q000187:drug effects; D017550:Spectroscopy, Fourier Transform Infrared; D014908:Triticum / Q000737:chemistry*
chemical_list: D004655:Emulsions; D005983:Glutens; D007444:Inulin; D005903:Gliadin; C037302:glutenin
keywords: Disulfide bonds; Emulsifying properties; Gliadin; Gluten; Glutenin; Inulin; Secondary structure