Thermal Aggregation of Hen Egg White Proteins in the Presence of Salts

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• 作者：Kazuki Iwashita ; Naoto Inoue ; Akihiro Handa ; Kentaro Shiraki
• 关键词：Hen egg white proteins ; Thermal aggregation ; Hofmeister series ; High concentration ; Crowding
• 刊名：The Protein Journal
• 出版年：2015
• 出版时间：June 2015
• 年：2015
• 卷：34
• 期：3
• 页码：212-219
• 全文大小：776 KB
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• 作者单位：Kazuki Iwashita (1)
  Naoto Inoue (1)
  Akihiro Handa (2)
  Kentaro Shiraki (1)
  
  1. Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8573, Japan
  2. R&D Division, Institute of Technology, Kewpie Corporation, 2-5-7 Sengawa, Chofu, Tokyo, 182-0002, Japan
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Bioorganic Chemistry
  Biochemistry
  Organic Chemistry
  Animal Anatomy, Morphology and Histology
  
• 出版者：Springer Netherlands
• ISSN：1573-4943

文摘

Hen egg white contains more than 40 kinds of proteins with concentrations reaching 100?mg/mL. Highly concentrated protein mixtures are common in the food industry, but the effects of a crowded environment containing salts on protein stability and aggregation have only been investigated using pure protein solutions. Here, we investigated the thermal aggregation of hen egg white protein (EWP) at various concentrations in the presence of inorganic salts by solubility measurements and SDS-PAGE. EWP at 1?mg/mL formed aggregates with increasing temperature above 55?°C; the aggregation temperatures increased in the presence of inorganic salt with the Hofmeister series. Namely, the chaotrope 0.5?M NaSCN completely suppressed the thermal aggregation of 1?mg/mL EWP. As the protein concentration increased, NaSCN unexpectedly enhanced the protein aggregation; the aggregation temperature of 10 and 100?mg/mL EWP solutions were dramatically decreased at 62 and 47?°C, respectively. This decrease in aggregation temperatures due to the chaotrope was described by the excluded volume effect, based on a comparative experiment using Ficoll 70 as a neutral crowder. By contrast, the kosmotrope Na₂SO₄ did not affect the aggregation temperature at concentrations from 1 to 100?mg/mL EWPs. The unexpected fact that a chaotrope rather enhanced the protein aggregation at high concentration provides new insight into the aggregation phenomena with the Hofmeister effect as well as the crude state of highly concentrated proteins.