Bacterial lipolytic enzymes, including carboxylesterases and lipases, are classified based on their amino acid sequences and biological properties. This review updates the classification of these enzymes into eight families, with the largest divided into six subfamilies. The classification is based on structural and functional characteristics, including the catalytic triad (Ser-Asp-His), disulphide bonds, and substrate specificity. The study highlights the structural diversity of these enzymes, such as the α/β-hydrolase superfamily, the GDSL family, and other families with distinct catalytic mechanisms. The paper discusses the properties of various bacterial lipases, including their secretion mechanisms, temperature preferences, and roles in industrial applications. It also addresses the challenges in classifying these enzymes due to their diversity and the limited information available in the literature. The study provides a comprehensive overview of bacterial lipases and esterases, aiding in the identification and characterization of novel enzymes. The classification is supported by data from protein and nucleotide databases, and the results are presented through sequence alignments and structural analysis. The paper emphasizes the importance of understanding the structural and functional diversity of these enzymes for their application in biotechnology and industrial processes.Bacterial lipolytic enzymes, including carboxylesterases and lipases, are classified based on their amino acid sequences and biological properties. This review updates the classification of these enzymes into eight families, with the largest divided into six subfamilies. The classification is based on structural and functional characteristics, including the catalytic triad (Ser-Asp-His), disulphide bonds, and substrate specificity. The study highlights the structural diversity of these enzymes, such as the α/β-hydrolase superfamily, the GDSL family, and other families with distinct catalytic mechanisms. The paper discusses the properties of various bacterial lipases, including their secretion mechanisms, temperature preferences, and roles in industrial applications. It also addresses the challenges in classifying these enzymes due to their diversity and the limited information available in the literature. The study provides a comprehensive overview of bacterial lipases and esterases, aiding in the identification and characterization of novel enzymes. The classification is supported by data from protein and nucleotide databases, and the results are presented through sequence alignments and structural analysis. The paper emphasizes the importance of understanding the structural and functional diversity of these enzymes for their application in biotechnology and industrial processes.