Combining non-in situ, in situ and molecular dynamics simulations to reveal the effects of ultra-high pressure on horseradish peroxidase
文献类型： 外文期刊
作者： Yang, Jiaxin 1 ; Zhang, Sinan 1 ; Lu, Han 3 ; Jin, Mingliang 5 ; Zheng, Haiyan 7 ; Cheng, Lina 8 ; Jiang, Zhuo 1 ;
作者机构： 1.South China Agr Univ, Coll Food Sci, Guangzhou 510642, Peoples R China
2.Zhejiang Univ, Coll Biosyst Engn & Food Sci, Hangzhou 310058, Zhejiang, Peoples R China
3.South China Normal Univ, Int Acad Optoelect Zhaoqing, Zhaoqing 526238, Peoples R China
4.Zhejiang Wanli Univ, Inst Carbon Neutral, Ningbo 315100, Peoples R China
5.South China Normal Univ, South China Acad Adv Optoelect, Guangzhou 510006, Peoples R China
6.South China Normal Univ, Natl Ctr Int Res Green Optoelect, Int Joint Lab Optofluid Technol & Syst, Guangzhou 510006, Peoples R China
7.Ctr High Pressure Sci & Technol Adv Res, Beijing 100193, Peoples R China
8.Guangdong Acad Agr Sci, Guangzhou 510642, Peoples R China
关键词： Horseradish peroxidase; Ultra-high pressure; In situ monitoring; Molecular dynamics simulation; Surface-enhanced Raman scattering
期刊名称：FOOD BIOSCIENCE （ 影响因子：5.9； 五年影响因子：6.1 ）
ISSN： 2212-4292
年卷期： 2025 年 65 卷
页码：
收录情况： SCI
摘要： To investigate the structure-activity relationship of horseradish peroxidase (HRP) under different pressure treatments, we employed a combination of non-in situ, in situ, and molecular dynamics simulations. In particular, we used a Diamond-Anvil Cell (DAC) and spectroscopic methods to study the structural changes of HRP under pressure from 0.1 MPa to 5.5 GPa in situ. The results showed that after being treated at 6 GPa, the enzyme activity of HRP remained at 7.04%. Between 3 and 4.5 GPa, there was a dramatic structural change. Pressure altered the volume, backbone, secondary structure, heme porphyrin ring, and hydrogen bonds of HRP, thereby reducing enzyme activity. This study reveals the mechanism by which pressure affects the structure-activity relationship of HRP.
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