首页> 外文期刊>Food Chemistry >Effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra
【24h】

Effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate using a newly developed approach in the analysis of difference-UV spectra

机译:加热,pH,超声和乙醇对乳清蛋白分离物变性的影响-使用最新开发的分析紫外光谱的方法

获取原文
获取原文并翻译 | 示例
           

摘要

A newly developed method of analysis of difference-UV spectra was successfully implemented in the study of the effect of heat, pH, ultrasonication and ethanol on the denaturation of whey protein isolate. It was found that whey proteins exhibit their highest stability against heat denaturation at pH 3.75. At very low pH values, i.e. 2.5, they exhibited considerable cold denaturation, while after heating at this pH value, the supplementary heat denaturation rate was lower compared to that at neutral pH. The highest heat denaturation rates were observed at pH values higher than neutral. High power sonication on whey proteins, previously heated at 90 degrees C for 30 min, resulted in a rather small reduction of the fraction of the heat denatured protein aggregates. Finally, when ethanol was used as a cosolvent in the concentration range 20-50%, a sharp increase in the degree of denaturation, compared to the native protein solution, was observed. (C) 2017 Elsevier Ltd. All rights reserved.
机译:在研究热,pH,超声和乙醇对乳清蛋白分离物变性的影响方面,成功地采用了新开发的差异紫外光谱分析方法。发现乳清蛋白在pH 3.75下表现出最高的抗热变性稳定性。在非常低的pH值下,即2.5,它们表现出相当大的冷变性,而在该pH值下加热后,其补充的热变性速率低于中性pH。在高于中性的pH值下观察到最高的热变性速率。先前在90摄氏度下加热30分钟的乳清蛋白的高能超声处理,导致热变性蛋白聚集体的比例降低了很小。最后,当使用乙醇作为助溶剂的浓度范围为20-50%时,与天然蛋白质溶液相比,观察到变性程度的急剧增加。 (C)2017 Elsevier Ltd.保留所有权利。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号