Oligoethylene glycols prevent thermal aggregation of α-chymotrypsin in a temperature-dependent manner : Implications for design guidelines.
Oligoethylene glycols prevent thermal aggregation of α-chymotrypsin in a temperature-dependent manner : Implications for design guidelines.
复制标题
低聚乙二醇以温度依赖性方式防止 α-胰凝乳蛋白酶的热聚集:对设计指南的影响。
DOI:
10.1002/btpr.1762
复制
发表时间:
2013
影响因子:
2.9
通讯作者:
Kentaro Shiraki
中科院分区:
文献类型:
--
作者:
Shunsuke Tomita;Yumiko Tanabe;Kentaro Shiraki
Protein aggregation is problematic in various fields, where aggregation can frequently occur during routine experiments. This study showed that tetraethylene glycol (TEG) and tetraethylene glycol dimethyl ether (TEGDE) act as aggregation suppressors that have different unique properties from typical additives to prevent protein aggregation, such as arginine (Arg) and NaCl. Thermal aggregation of α‐chymotrypsin was well suppressed with the addition of both TEG and TEGDE. Interestingly, the suppressive effects of Arg and NaCl on thermal aggregation were almost unchanged when temperature was shifted from 65°C to 85°C, whereas both TEG and TEGDE significantly decreased the aggregation rate with increasing temperature. Note that the effects of TEG and TEGDE were higher than Arg above 75°C. This temperature‐dependent behavior of TEG and TEGDE provides a novel design guideline to develop aggregation suppressors for use at high temperature, i.e., the importance of the ethylene oxide group. © 2013 American Institute of Chemical EngineersBiotechnol. Prog., 29:1325–1330, 2013