Sequence Analysis and In Silico Characterization of Lipase from Acinetobacter gerneri CE4.3 and PKY2.2

Lipase is an enzyme that catalyzes the breakdown of fats into fatty acids and glycerol. Lipase plays a crucial role in various industries. Bacterial lipases are widely studied and utilized in the biotechnology industry because of their adaptability, efficiency in large-scale production, and abundance in lipid-rich environments. The objectives of this research were to isolate and identify lipase-producing bacteria from grease traps in canteens at the University of Phayao. The bacterial isolates were analyzed for the lipase gene through PCR amplification and sequencing. Characteristics of the lipase protein were predicted through in silico studies. The results revealed that the two isolates were Acinetobacter gerneri (A. gerneri) CE4.3 and PKY2.2, which contain the lipase lip50 and lip66 genes. The nucleotide sequences of the lipase genes and amino acid sequences in both strains showed high similarity to the A. gerneri DSM 14967 (EPR83194.1). The predicted physicochemical properties of Lip50 and Lip66 proteins from both strains indicate that they are slightly basic, thermostable, and hydrophilic. Lip50 and Lip66 proteins of both strains contain conserved domains of the lipase enzyme. The analysis of the phylogenetic tree and multiple sequence alignment of Lip50 and Lip66 proteins from both strains indicated that they belong to lipase family V. In conclusion, Lip50 and Lip66 from A. gerneri CE4.3 and PKY2.2 are the foundations for the study of lipase enzymes for biotechnology. HIGHLIGHTSLipase-producing bacteria isolated from grease traps of canteens at the University of Phayao were identified as Acinetobacter gerneri (A. gerneri) CE4.3 and PKY2.2. Both strains possess lipase genes (lip50 and lip66), which encode proteins (Lip50 and Lip66) containing conserved domains essential for lipase activity. Phylogenetic analysis, together with multiple sequence alignment, indicates that these proteins belong to lipase family V. This study provides fundamental information supporting further research and the potential biotechnological applications of lipase enzymes from A. gerneri. GRAPHICAL ABSTRACT