Bacterial alkaline proteases are essential for cell growth and differentiation and are widely used in various industrial sectors. These enzymes are commercially available, such as subtilisin Carlsberg, subtilisin BPN', and Savinase, primarily used in the detergent industry. Mutations have led to improved protease preparations with better catalytic efficiency and stability. Newer proteases like Durazym, Maxapem, and Purafect have been developed using site-directed and random mutagenesis. Directed evolution has produced various subtilisin variants with better specificity and stability. Molecular imprinting through lyophilization is emerging as a method in protein engineering. The search for novel alkaline proteases through metagenomics is targeting undiscovered molecular diversity, allowing biotechnological exploitation of uncultured microorganisms. Proteases account for about 40% of total enzyme sales in various industries, with detergent alkaline proteases being the largest share. Microbial proteases are classified based on their activity under different pH conditions and active site characteristics. Alkaline proteases are active in neutral to alkaline pH ranges and are either serine or metallo-type. Serine proteases are of considerable interest due to their activity and stability at alkaline pH, with applications in various industries. They have a nucleophilic serine residue in their active site and a catalytic triad of aspartate, histidine, and serine. They are generally active at neutral and alkaline pH, with optima at pH 7–11. Chymotrypsin-like proteases are specific for basic amino acids and are most active at pH 8. Subtilisin-like proteases are generally bacterial in origin and secreted extracellularly. They are specific for aromatic or hydrophobic residues and active around pH 10. Wheat serine carboxypeptidase II-like proteases are active in pH range 4.5–5.5, suggesting a low pKa for their catalytic histidine residue.Bacterial alkaline proteases are essential for cell growth and differentiation and are widely used in various industrial sectors. These enzymes are commercially available, such as subtilisin Carlsberg, subtilisin BPN', and Savinase, primarily used in the detergent industry. Mutations have led to improved protease preparations with better catalytic efficiency and stability. Newer proteases like Durazym, Maxapem, and Purafect have been developed using site-directed and random mutagenesis. Directed evolution has produced various subtilisin variants with better specificity and stability. Molecular imprinting through lyophilization is emerging as a method in protein engineering. The search for novel alkaline proteases through metagenomics is targeting undiscovered molecular diversity, allowing biotechnological exploitation of uncultured microorganisms. Proteases account for about 40% of total enzyme sales in various industries, with detergent alkaline proteases being the largest share. Microbial proteases are classified based on their activity under different pH conditions and active site characteristics. Alkaline proteases are active in neutral to alkaline pH ranges and are either serine or metallo-type. Serine proteases are of considerable interest due to their activity and stability at alkaline pH, with applications in various industries. They have a nucleophilic serine residue in their active site and a catalytic triad of aspartate, histidine, and serine. They are generally active at neutral and alkaline pH, with optima at pH 7–11. Chymotrypsin-like proteases are specific for basic amino acids and are most active at pH 8. Subtilisin-like proteases are generally bacterial in origin and secreted extracellularly. They are specific for aromatic or hydrophobic residues and active around pH 10. Wheat serine carboxypeptidase II-like proteases are active in pH range 4.5–5.5, suggesting a low pKa for their catalytic histidine residue.