Effect of ionic strength (NaCl and CaCl2) on functional, textural and electrophoretic properties of native and acetylated gluten, gliadin and glutenin

被引:23
作者
Abedi, Elahe [1 ]
Majzoobi, Mahsa [2 ,3 ,4 ]
Farahnaky, Asgar [2 ,5 ,6 ]
Pourmohammadi, Kiana [1 ]
Mahmoudi, Mohammad Reza [7 ]
机构
[1] Fasa Univ, Dept Food Sci & Technol, Fasa, Iran
[2] Shiraz Univ, Sch Agr, Dept Food Sci & Technol, Shiraz, Iran
[3] Wagga Wagga Agr Inst, NSW Dept Primary Ind, Wagga Wagga, NSW 2650, Australia
[4] Graham Ctr Agr Innovat, Wagga Wagga, NSW 2650, Australia
[5] Charles Sturt Univ, ARC Ind Transformat Training Ctr Funct Grains, Sch Biomed Sci, Wagga Wagga, NSW 2650, Australia
[6] Charles Sturt Univ, Graham Ctr Agr Innovat, Wagga Wagga, NSW 2650, Australia
[7] Fasa Univ, Dept Stat, Fasa, Iran
关键词
Acetylation; Ionic strength; Gliadin; Glutenin; Texture property; SDS PAGE; DYNAMIC RHEOLOGICAL PROPERTIES; WHEAT-FLOUR DOUGH; FOAMING PROPERTIES; SODIUM-CHLORIDE; CROSS-LINKING; PROTEIN; PH; CONFORMATION; FRACTIONS; CULTIVARS;
D O I
10.1016/j.ijbiomac.2018.09.155
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The main objective of this study was to determine the effects of different ionic strengths (IS) of NaCI and CaCl2 (0.2, 0.4 and 0.6 at pH = 7) on the functional (water holding capacity (WHC), water absorption (WA), emulsifying activity (EA), emulsion stability (ES), textural and electrophoretical properties of native (N) and acetylated (AC) gluten, gliadin and glutenin. According to FT-IR and TNBS methods, the modification extent of wheat gliadin and glutenin were somewhat lower and higher than gluten, respectively. The results indicating that functionality AC glutenin was more than AC gluten and gliadin. NaCI and CaCl2 had negative impact on WHC, WA, EA and ES of proteins. Different IS of NaCI and CaCl2 may only alter the molecular conformation of N and AC gluten, gliadin and glutenin without having any significant effect on the molecular weights of these proteins. AC proteins had significantly higher WHC of gels compared to N proteins and also, CaCl2 could enhance the WHC and hardness of N and AC protein compared with NaCI. Hardness of AC glutenin more impressed than gliadin and gluten due to high degree acetylation. (C) 2018 Published by Elsevier B.V.
引用
收藏
页码:2035 / 2047
页数:13
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