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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Effect of ionic strength (NaCl and CaCl2) on functional, textural and electrophoretic properties of native and acetylated gluten, gliadin and glutenin
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Effect of ionic strength (NaCl and CaCl2) on functional, textural and electrophoretic properties of native and acetylated gluten, gliadin and glutenin

机译：离子强度（NaCl和CaCl2）对天然和乙酰化谷蛋白，Gliadin和谷蛋白的功能性，纹理和电泳性能的影响

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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.
机译：本研究的主要目的是确定不同离子强度（IS）的NaCl和CaCl 2（0.2,0.4和0.6at在pH = 7）上的效果（水持能力（WHC），吸水（WA），乳化活性（EA），乳液稳定性（ES），天然（N）和乙酰化（AC）谷蛋白，胶质苷和谷蛋白的纹理和电泳性能。根据FT-IR和TNBS方法，小麦胶质素和谷蛋白的改性程度分别略低，高于麸质。结果表明官能度AC氨基丁蛋白的结果不仅仅是AC麸质和Gliadin。NaCl和CaCl2对蛋白质的WHC，WA，EA和ES产生负面影响。不同的是NaCl和CaCl2只能改变N和Ac面筋，胶质苷和谷蛋白对这些蛋白质的分子量没有任何显着影响的分子构象。与N蛋白相比，Ac蛋白的凝胶显着高，CaCl2可以增强WHC和康登斯与NaCl相比，N和AC蛋白的S. AC氨基蛋白的硬度比Gliadin和由于高级乙酰化因胶质蛋白和麸质而言更为印象。 （c）2018由elestvier b.v出版。

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