Modification of protein structure and dough rheological properties of wheat flour through superheated steam treatment |
| |
Affiliation: | 1. Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos, Rua Monteiro Lobato, 80, CEP 13083-862, Cidade Universitária Zeferino Vaz, Campinas, São Paulo, Brazil;2. Instituto Federal de Educação, Ciência e Tecnologia Farroupilha, Rua Venâncio Aires, 822, CEP 97541-500, Alegrete, Rio Grande do Sul, Brazil;1. Institute of Agro-Products Processing Science and Technology, Chinese Academy of Agriculture Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China;2. Bruker (Beijing) Scientific Technology Co., Ltd., Beijing 100081, PR China;1. University of Liège, Gembloux Agro-Bio Tech, Care FoodIsLifeFood, Science and Formulation Unit, Avenue de la Faculté 2B, B-5030, Gembloux, Belgium;2. University of Liège, Gembloux Agro-Bio Tech, Care FoodIsLife, Avenue de la Faculté 2B, B-5030, Gembloux, Belgium;3. Moulins de Statte SA, Belgium;4. Wal.Agri SA, Belgium;5. Walloon Agricultural Research Center, Unit of Products Transformation Technology, 24 Chaussée de Namur, 5030, Gembloux, Belgium |
| |
Abstract: | Native (NF, 13.5% w.b) and moistened (MF, 27% w.b) wheat flours were treated with superheated steam (SS) at 170 °C for 1, 2 and 4 min, and their protein structure as well as dough rheological properties were analyzed. Confocal laser scanning microscopy (CLSM) and SDS-PAGE patterns indicated the formation of protein aggregates with reduced SDS extractability after treatment. Farinograph and dynamic rheometry measurements showed that the strength as well as elastic and viscous moduli of the dough made from SS-treated flours progressively increased with SS treatment time. And both the improvements were more pronounced for superheated steam-treated moistened flours (SS-MF) than for superheated steam-treated native flours (SS-NF). Size-exclusion high performance liquid chromatography (SE-HPLC) analysis demonstrated that dough rheological parameters have positive correlations with SDS unextractable polymeric proteins (UPP) contents. SS treatment on flours led to a transition of protein secondary structures to more ordered form (α-helix and β-sheet). Additionally, free sulfhydryl (SH) contents decreased after treatment, which implied that disulfide bonds accounted for protein extractability loss and dough rheological properties improvement. Elevated moisture level promoted the modification of both protein structure and dough behaviors of flours during SS treatment. |
| |
Keywords: | Superheated steam Wheat flour Protein structure Dough rheological properties NF" },{" #name" :" keyword" ," $" :{" id" :" kwrd0035" }," $$" :[{" #name" :" text" ," _" :" native wheat flour MF" },{" #name" :" keyword" ," $" :{" id" :" kwrd0045" }," $$" :[{" #name" :" text" ," _" :" moistened wheat flour SS" },{" #name" :" keyword" ," $" :{" id" :" kwrd0055" }," $$" :[{" #name" :" text" ," _" :" superheated steam SS-NF" },{" #name" :" keyword" ," $" :{" id" :" kwrd0065" }," $$" :[{" #name" :" text" ," _" :" superheated steam-treated native flour SS-MF" },{" #name" :" keyword" ," $" :{" id" :" kwrd0075" }," $$" :[{" #name" :" text" ," _" :" superheated steam-treated moistened flour CLSM" },{" #name" :" keyword" ," $" :{" id" :" kwrd0085" }," $$" :[{" #name" :" text" ," _" :" confocal laser scanning microscopy SDS-PAGE" },{" #name" :" keyword" ," $" :{" id" :" kwrd0095" }," $$" :[{" #name" :" text" ," _" :" sodium dodecyl sulphate-polyacrylamide gel electrophoresis SE-HPLC" },{" #name" :" keyword" ," $" :{" id" :" kwrd0105" }," $$" :[{" #name" :" text" ," _" :" size-exclusion high performance liquid chromatography UPP" },{" #name" :" keyword" ," $" :{" id" :" kwrd0115" }," $$" :[{" #name" :" text" ," _" :" unextractable polymeric proteins SH" },{" #name" :" keyword" ," $" :{" id" :" kwrd0125" }," $$" :[{" #name" :" text" ," _" :" sulfhydryl HMW-GS" },{" #name" :" keyword" ," $" :{" id" :" kwrd0135" }," $$" :[{" #name" :" text" ," _" :" high molecular weight glutenins subunits LMW-GS" },{" #name" :" keyword" ," $" :{" id" :" kwrd0145" }," $$" :[{" #name" :" text" ," _" :" low molecular weight glutenins subunits FITC" },{" #name" :" keyword" ," $" :{" id" :" kwrd0155" }," $$" :[{" #name" :" text" ," _" :" Fluorescein isothiocyanate FTIR" },{" #name" :" keyword" ," $" :{" id" :" kwrd0165" }," $$" :[{" #name" :" text" ," _" :" Fourier transform infrared spectroscopy SD" },{" #name" :" keyword" ," $" :{" id" :" kwrd0175" }," $$" :[{" #name" :" text" ," _" :" standard deviation |
本文献已被 ScienceDirect 等数据库收录! |
|