Investigation on the interaction of catalase with sodium lauryl sulfonate and the underlying mechanisms |
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Authors: | Jing Wang Rui Jia Jiaxi Wang Zhiqiang Sun Zitao Wu Rutao Liu Wansong Zong |
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Affiliation: | 1. School of Environmental and Material Engineering, Yantai University, Yantai 264005, People's Republic of China;2. Research Center of Hydrobiology, Jinan University, Guangzhou, People's Republic of China;3. School of Environmental Science and Engineering, China ‐ America CRC for Environment & Health, Shandong University, Jinan 250100, People's Republic of China;4. College of Population, Resources and Environment, Shandong Normal University, Jinan 250014, People's Republic of China |
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Abstract: | As a classic type of anionic surfactants, sodium lauryl sulfonate (SLS) might change the structure and function of antioxidant enzyme catalase (CAT) through their direct interactions. However, the underlying molecular mechanism is still unknown. This study investigated the direct interaction of SLS with CAT molecule and the underlying mechanisms using multi‐spectroscopic methods, isothermal titration calorimetry, and molecular docking studies. No obvious effects were observed on CAT structure and activity under low SLS concentration exposure. The particle size of CAT molecule decreased and CAT activity was slightly inhibited under high SLS concentration exposure. SLS prefers to bind to the interface of CAT mainly via van der Waals’ forces and hydrogen bonds. Subsequently, SLS interacts with the amino acid residues around the heme groups of CAT via hydrophobic interactions and might inhibit CAT activity. |
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Keywords: | catalase molecular mechanisms sodium lauryl sulfonate toxicity evaluation |
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