Thermal aggregation of hen egg white proteins in the presence of salts.
Thermal aggregation of hen egg white proteins in the presence of salts.
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DOI：
10.1007/s10930-015-9612-3
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发表时间：
2015-06
期刊：
影响因子：
3
通讯作者：
Shiraki, Kentaro
中科院分区：
文献类型：
--
作者：
Iwashita, Kazuki;Inoue, Naoto;Handa, Akihiro;Shiraki, Kentaro
鸡蛋白色中含有40多种蛋白质，蛋白质浓度达100 mg/mL。高度浓缩的蛋白质混合物在食品工业中很常见，但仅使用纯蛋白质溶液研究了含盐的拥挤环境对蛋白质稳定性和聚集的影响。在此，我们研究了鸡蛋白色蛋白（EWP）在不同浓度的无机盐存在下，通过溶解度测量和SDS-PAGE的热聚集。1 mg/mL的EWP随温度升高至55 °C以上形成聚集体;在无机盐存在下，聚集温度升高，具有Hofmeister系列。即，离液剂0.5 M NaSCN完全抑制1 mg/mL EWP的热聚集。随着蛋白质浓度的增加，NaSCN意外地增强了蛋白质聚集; 10和100 mg/mL EWP溶液的聚集温度分别在62和47 °C下急剧降低。基于使用Ficoll 70作为中性拥挤剂的比较实验，通过排除的体积效应描述了由于离液剂引起的聚集温度的这种降低。相比之下，kosmotrope Na 2SO 4在1至100 mg/mL EWP的浓度下不影响聚集温度。离液剂在高浓度下相当增强蛋白质聚集的意外事实提供了对具有Hofmeister效应的聚集现象以及高浓度蛋白质的粗状态的新见解。
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.
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影响因子：
5.6
作者：
Kozer, N;Schreiber, G
通讯作者：
Schreiber, G
DOI：
10.1107/s1744309110013710
发表时间：
2010-06-01
影响因子：
0.9
作者：
Ito, Len;Shiraki, Kentaro;Yamaguchi, Hiroshi
通讯作者：
Yamaguchi, Hiroshi
影响因子：
2.9
作者：
Matsuoka, Tsuneyoshi;Hamada, Hiroyuki;Shiraki, Kentaro
通讯作者：
Shiraki, Kentaro
DOI：
10.1046/j.1432-1033.2003.03850.x
发表时间：
2003-11-01
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
Kudou, M;Shiraki, K;Takagi, M
通讯作者：
Takagi, M
影响因子：
3
作者：
Hirano, Atsushi;Hamada, Hiroyuki;Shiraki, Kentaro
通讯作者：
Shiraki, Kentaro