Species Relationship and Structural Prediction Based on Lipase Gene of A Thermohalophilic Bacterium PLS A
Lipase Gene of A Thermohalophilic Bacterium PLS A
DOI:
https://doi.org/10.25077/jrk.v17i2.867Keywords:
PLS A, lipase gene, thermo-halophilicAbstract
Lipase is a hydrolase enzyme that catalyses the hydrolysis of triacylglycerol into glycerol and free fatty acids. It has broad industrial applications, including in the detergent, papermaking, leather, and food industries. This study aimed to predict the structure of the lipase enzyme encoded by a gene from a thermophilic bacterial isolate, Pria Laot Sabang A (PLS A), obtained from undersea fumaroles in Pria Laot Sabang, Weh Island, Aceh, Indonesia. The lipase gene was amplified using the Polymerase Chain Reaction (PCR) method with a specific primer pair (Flip2-Rlip2), resulting in a gene of ± 1300 bp. Homology analysis of the same genes in NCBI showed that the PLS A lipase gene was highly similar to that of Geobacillus thermoleovorans strain ARTRW1. However, phylogenetic analysis indicated that PLS A formed a distinct branch. The lipase structure was predicted using the SWISS-MODEL server, which showed the highest structural similarity to the lipase of the G. zalihae strain T1. The predicted protein structure revealed the presence of Zn²⁺ and Ca²⁺ ions, suggesting that the lipase from PLS A is a metalloenzyme. The protein structure of PLS A also indicated high stability, highlighting its potential for industrial applications.
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