The enzyme urease is crucial for a process called microbial-induced calcium carbonate precipitation (MICP). This process is important because it helps in forming calcium carbonate, which is useful in various environmental and industrial applications. However, using MICP in extreme environments, like acidic mine drainage or industrial waste sites, is challenging. This is because scientists do not fully understand how urease behaves in such harsh conditions.

Researchers decided to tackle this issue by combining lab experiments with a technique called constant pH molecular dynamics (CpHMD) simulations. They wanted to see how different pH levels (ranging from 3 to 11) affect the structure of urease from the bacterium Sporosarcina pasteurii. Specifically, they focused on the α-subunit of urease, which is a key part of the enzyme.

The experiments showed that urease works best at a pH level between 7 and 8. This finding was supported by the molecular dynamics results, which indicated that urease maintains its structure and function best in neutral to slightly alkaline conditions. In contrast, extreme pH levels (3, 4, and 11) caused significant disruptions in the enzyme's active site, leading to impaired function.

The CpHMD simulations provided additional insights. They showed that the α-subunit of urease can retain its structure at optimal pH levels, suggesting that it might be able to reassemble after experiencing environmental stress. This discovery is important because it helps bridge the gap in understanding how enzymes like urease can remain stable in harsh conditions.

Understanding how urease behaves under different pH conditions is crucial for optimizing MICP in various applications. This includes geotechnical engineering and environmental remediation, where the process can be used to stabilize soils or clean up contaminated sites. By gaining a better understanding of urease's behavior, scientists can develop more effective strategies for using MICP in these challenging environments.

How pH Levels Impact Urease in Bacteria

Actions