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作 者:张倩 陈复生[1] ZHANG Qian;CHEN Fusheng(College of Food Science and Technology,Henan University of Technology,Zhengzhou 450001,China)
机构地区:[1]河南工业大学粮油食品学院,河南郑州450001
出 处:《食品科学》2019年第7期108-113,共6页Food Science
基 金:国家自然科学基金面上项目(21676073;21376064);河南省优秀科技创新团队项目;中国博士后科学基金项目(2015M582184);河南自然科学基金重点项目(162300410046)
摘 要:目的:大豆蛋白提取方法的深入研究能够在一定程度上为植物蛋白的开发利用提供新可能。本研究以常规碱溶酸沉法为对照,与反胶束法提取得到的蛋白质差异进行全面对比,进而探讨反胶束萃取环境的独特作用。方法:以全脂大豆粉为原料,分别采用反胶束法和碱溶酸沉法制备大豆分离蛋白,并进一步对比两种方法得到的大豆分离蛋白的结构、热力学和流变学特性。结果:反胶束法得到的大豆分离蛋白的β-折叠结构含量较低,β-转角结构含量较高,蛋白展开程度较低,具有较低的表面疏水性,相较于传统碱溶酸沉法能够较好地保持蛋白质的天然分子结构;反胶束法得到的蛋白质的热稳定性较差,更易于形成凝胶,但所形成的凝胶强度较低。结论:反胶束萃取环境独特的水核结构能够较好地保持大豆分离蛋白的天然分子结构。More intensive research on the extraction of soybean protein isolate (SPI) may provide new possibilities for developing and utilizing plant proteins. In this study we made a comprehensive comparison between traditional alkali dissolution and acid precipitation method and reverse micellar extraction (RME) for soybean protein extraction and we investigated the unique properties of the reverse micellar environment. For this purpose, the structure, thermodynamic properties and rheological properties of SPI extracted from full-fat soybean powder by the two methods were studied. The results demonstrated that the SPI extracted by RME contained less β-sheet but more β-turn structure, representing a higher degree of unfolding, and therefore had a lower surface hydrophobicity. The reverse micelle environment could protect the protein from denaturation by organic solvents. The SPI extracted by RME had poor thermostability and was more prone to gelation, but the gel strength was lower when compared with the SPI extracted by the traditional method. Finally, we came to the conclusion that the unique water core structure of the reverse micelle could help to preserve the native structure of SPI.
关 键 词:反胶束 大豆分离蛋白 分子结构 热力学特性 流变学特性
分 类 号:TS214.2[轻工技术与工程—粮食、油脂及植物蛋白工程]
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