Halophilic bacteria thrive in environments with high concentrations of sodium chloride, such as salt mines, solar salterns, and hypersaline lakes. They survive extreme salinity by balancing osmotic pressure, preventing cellular damage. Extreme halophiles require up to 30 % salt for growth and structural integrity, making their proteins uniquely stable and functional in high-salt conditions. Understanding the molecular mechanisms behind halophilic protein stability is crucial for biotechnology. Investigating halotolerant proteins can lead to novel industrial applications, including enzymes for food processing, bioremediation, and pharmaceuticals. Proteomics, the large-scale study of proteins, helps characterize the proteomes of halophilic bacteria. Recent advancements in proteomic techniques allow deeper insights into protein structure, function, and adaptation in hypersaline environments. Modern methods, such as mass spectrometry and two-dimensional gel electrophoresis, facilitate the identification and analysis of halophilic proteins. This review explores advanced proteomic tools for studying halophilic bacteria, shedding light on protein stability, molecular mechanisms, and biotechnological potential. Understanding these proteins paves the way for innovations in enzyme engineering, industrial biotechnology, and synthetic biology. By leveraging cutting-edge proteomics, researchers can unlock new applications for halophilic proteins across industries, enhancing sustainability and efficiency in extreme environments.
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