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Novel Thermostable Manganese Superoxide Dismutase from Alicyclobacillus sp. with High Specific Activity and Antioxidant Properties

文献类型： 外文期刊

作者： Sun, Xihang 1 ; Liu, Jinping 1 ; Ge, Qianqian 1 ; Jiang, Yayun 1 ; Xu, Yi 1 ; Li, Yuying 1 ; Hou, Zhenping 1 ; Shi, Pengjun 1 ;

作者机构： 1.Chinese Acad Agr Sci, Inst Bast Fiber Crops, Changsha 410205, Hunan, Peoples R China

2.Hunan Agr Univ, Coll Anim Sci & Technol, Changsha 410000, Hunan, Peoples R China

关键词： superoxide dismutase; specific activity; thermostability; antioxidation; IPEC-J2 cell

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.2； 五年影响因子：6.4 ）

ISSN： 0021-8561

年卷期： 2025 年 73 卷 10 期

页码：

收录情况： SCI

摘要： Superoxide dismutase (SOD) is a vital antioxidant enzyme that exerts antioxidative and anti-inflammatory effects on the host. In this study, a novel thermostable SOD of Alicyclobacillus sp. (AliSOD) from a hot spring was overexpressed in Escherichia coli, and enzymatic properties were identified. Mn2+ plays a decisive role in enzyme activity, indicating that AliSOD is MnSOD. Specifically, AliSOD was determined to be dimeric with a subunit molecular mass of 23.0 kDa, and the specific activity was confirmed to be as high as 24990.8 Umg(-1). AliSOD demonstrated exceptional thermal stability, broad pH stability, and resistance to urea, exhibiting minimal loss of activity at 70 degrees C and remarkable tolerance in an alkaline environment. Moreover, AliSOD significantly alleviated oxidative stress in diquat-injured cells (P < 0.01). It also increased intracellular SOD expression and activated the Nrf2 protein downstream of the Keap1-Nrf2 signaling pathway (P < 0.05). Overall, AliSOD exhibits excellent thermostability and specific activity, indicating potential applications in the pharmaceutical, food, and animal feed industries.

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