New insights into the functionality of protein to the emulsifying properties of sugar beet pectin
New insights into the functionality of protein to the emulsifying properties of sugar beet pectin
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DOI：
10.1016/j.foodhyd.2016.02.005
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发表时间：
2016-06-01
影响因子：
10.7
通讯作者：
Yin, Lijun
中科院分区：
文献类型：
--
作者：
Chen, Hao;Qiu, Shuang;Yin, Lijun
蛋白质对甜菜果胶的乳化性能有重要影响。研究了蛋白质含量及蛋白质与果胶的结合方式对SBP乳化性能的影响。结果表明，SBPs的蛋白质含量和结构差异影响乳状液的稳定性。随着蛋白质含量从0.5%增加到3.0%，SBP稳定的乳状液液滴尺寸急剧减小。当蛋白质含量增加到较高水平（3.0 ~ 6.0%）时，酶活性趋于稳定。热重分析证实了SBP样品之间的结构差异。为了研究蛋白质/果胶组合方式对乳化性能的影响，通过去除部分蛋白质，将BSA静电或共价结合到脱蛋白的SBP上，对SBP进行修饰。结果表明，与原SBP、去蛋白SBP和静电键合复合物相比，美拉德诱导的复合物具有最好的乳化稳定性。这些结果表明，蛋白质含量和蛋白质与果胶的结合方式均会影响SBP的乳化性能。(C)2016爱思唯尔有限公司版权所有
Protein plays an important role in the emulsifying properties of sugar beet pectin (SBP). The present work was carried out to investigate the role of protein content and the combination mode between proteins and pectins on the emulsifying properties of SBP. It was found that protein contents and structural differences of SBPs affected the stability of emulsion. As the protein content increased from 0.5 to 3.0%, droplet size of emulsion stabilized by SBP decreased sharply. It turned to be stable when the protein content increased to a high level (from 3.0 to 6.0%). Thermal gravimetric analysis confirmed the structural differences among SBP samples. In order to study the functionality of protein/pectin combination mode to emulsifying properties, modification of SBP was conducted by depleting a portion of proteins, and electrostaticly or covalently binding BSA to the de-proteinized SBP. Results showed that Maillard induced conjugates exhibited the best emulsifying stability, as compared with original SBP, deproteinized SBP and the electrostatic bonding complex. These results suggested that both protein content and the combination mode between protein and pectin could affect the emulsifying properties of SBP. (C) 2016 Elsevier Ltd. All rights reserved.