Charoensri_2025_Trends.Sci_22_10584

Lipase is an enzyme that catalyzes the breakdown of fats into fatty acids and glycerol. Lipase plays a crucial role in various industries. Bacterial lipasesarewidely studied and utilized in the biotechnology industry because of theiradaptability, 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 incanteens 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 andPKY2.2, which contain the lipase lip50 and lip66 genes. The nucleotide sequences of the lipase genes and amino acid sequences inboth strains showed high similarity to the A. gerneriDSM 14967 (EPR83194.1). The predicted physicochemical propertiesof Lip50 andLip66proteins from both strains indicate that they areslightly 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. gerneriCE4.3 and PKY2.2 are the foundations for the study of lipase enzymes for biotechnology