黄韫琪,杨晓泉.小麦蛋白组分调节改善乳液的稳定性及消化特性[J].,2020,36(6):198-203.
小麦蛋白组分调节改善乳液的稳定性及消化特性
Improvement of Emulsion Stability and Digestion Properties by Adjusting Wheat Protein Composition
投稿时间:2019-10-08  
DOI:10.13982/j.mfst.1673-9078.2020.6.0969
中文关键词:  麦醇溶蛋白  麦谷蛋白  乳液  稳定  消化
英文关键词:gliadin  glutenin  emulsion  stability  digestion
作者简介:黄韫琪(1995-),女,硕士研究生,研究方向:植物蛋白工程 通讯作者:杨晓泉(1965-),男,博士,教授,研究方向:植物蛋白质的开发与利用
基金项目:国家自然科学基金项目(31771923)
作者单位
黄韫琪 (华南理工大学食品科学与工程学院食物蛋白与胶体研究中心,广东省天然产物绿色加工与产品安全重点实验室,广东广州 510640) 
杨晓泉  
AuthorInstitution
HUANG Yun-qi (Laboratory of Food Proteins and Colloids, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China) 
YANG Xiao-quan (Laboratory of Food Proteins and Colloids, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China) 
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中文摘要:
      本研究通过调节麦醇溶蛋白和麦谷蛋白的比例,构建结构稳定且能够延缓脂肪释放的小麦蛋白基食品乳液体系。结果表明,在小麦蛋白组分当中,麦醇溶蛋白具有良好的界面性质,能形成稳定的界面层,麦谷蛋白的界面活性虽然较差,但其能够在界面上形成强有力的网络支撑,保护乳液不受外界环境的干扰。相比于单独小麦蛋白稳定的乳液,经组分调节后的复合蛋白具有较低的界面张力,可形成致密的纤维状蛋白界面层及较小的乳液液滴。当麦醇溶蛋白和麦谷蛋白的比例为1:2时,乳液在4 ℃贮藏1个月或经90 ℃加热30 min后粒度基本保持在28.33 μm左右,其贮藏稳定性和热稳定性也显著提高。此外,小麦蛋白组分间通过界面协同作用形成的复合界面层在胃肠消化过程中难以被胆盐和胰脂肪酶所取代。因此,通过小麦蛋白组分调节可改善乳液稳定性并一定程度上抑制脂肪在乳液中的消化速率。
英文摘要:
      In this study, wheat protein-based food emulsion system with stable structure and delayed lipid digestion were constructed by controlling the gliadin-to-glutenin ratio. The results showed that among the wheat protein components, gliadin had good interfacial properties, and could form a stable interfacial layer. Although the interfacial activity of glutenin was poor, it could form a strong network at the interface and protect the emulsion from external environmental disturbances. Compared with the pure gluten-based emulsion, the composite protein with a controlled wheat protein composition had lower interfacial tension, forming a dense fibrous protein interfacial layer and smaller emulsion droplets. When the ratio of gliadin to glutenin was 1:2, the droplet size of emulsion samples remained 28.33 μm after 1 month of storage at 4 ℃or after being heated at 90 ℃ for 30 min, with the storage stability and thermal stability of emulsions being improved significantly. In addition, the complex interfacial layer formed by interfacial synergy between wheat protein components was difficult to be replaced by bile salts and pancreatic lipase during gastrointestinal digestion. Therefore, the stability of the emulsion could be improved and the digestion rate of the lipids in the emulsion could be inhibited to some extent by controlling the wheat protein composition.
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