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

• DOI: 10.1021/acs.jafc.4c09697
• Publication Date: 2025-02-27T20:32:01Z
• Authors: Xihang Sun; Jinping Liu; Qianqian Ge; Yayun Jiang; Yi Xu; Yuying Li; Zhenping Hou; Pengjun Shi

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