Isolation, Purification, and Properties of a Novel Small Heat Shock Protein from the Hyperthermophile Sulfolobus solfataricus

Isolation, Purification, and Properties of a Novel Small Heat Shock Protein from the Hyperthermophile Sulfolobus solfataricus
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超嗜热硫磺菌中新型小热休克蛋白的分离、纯化和性质

DOI:
10.1007/s12010-009-8809-3
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发表时间:
2010-09
影响因子:
3
通讯作者:
--
中科院分区:
工程技术3区
文献类型:
--
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对来自超嗜热古菌硫磺菌硫化叶菌的一种假定的小热休克蛋白 (sHsp)(名为 SsHSP14.1)的分离、纯化和特性进行了研究。 sHsp 已成功从大肠杆菌中表达并纯化。研究了 SsHSP14.1 在加热过程中防止蛋白质聚集的体内伴侣功能。研究发现,分子量为 17.8 kDa 的重组 SsHSP14.1 可阻止大肠杆菌蛋白在 50 摄氏度下体内聚集。这一结果表明,SsHSP14.1 通过阻止蛋白质在超适温度下聚集,赋予嗜温细菌生存优势。在体外,纯化的 SsHSP14.1 蛋白能够在 80 摄氏度下阻止南极假丝酵母脂肪酶 B 聚集长达 60 分钟。此外,SsHSP14.1 增强了菠萝蛋白酶的热稳定性,使其在 55 摄氏度下的半衰期延长了 67%。
The isolation, purification, and properties of a putative small heat shock protein (sHsp), named SsHSP14.1, from the hyperthermophilic archaeon Sulfolobus solfataricus have been investigated. The sHsp was successfully expressed and purified from Escherichia coli. In vivo chaperone function of SsHSP14.1 for preventing aggregation of proteins during heating was investigated. It was found that recombinant SsHSP14.1 with a molecular mass of 17.8 kDa prevented E. coli proteins from aggregating in vivo at 50 degrees C. This result suggested that SsHSP14.1 confers a survival advantage on mesophilic bacteria by preventing protein aggregation at supraoptimal temperatures. In vitro, the purified SsHSP14.1 protein was able to prevent Candida antarctica lipase B from aggregation for up to 60 min at 80 degrees C. Moreover, the SsHSP14.1 enhanced thermostability of bromelain extending its half-life at 55 degrees C by 67%.
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