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Bacterial hormone-sensitive lipases (bHSLs), which are homologous to the catalytic domains of human HSLs, have received great interest due to their uses in the preparation of highly valuable biochemicals, such as drug intermediates or chiral building blocks. Here, a novel cold-active HSL from Halocynthiibacter arcticus ( Ha HSL) was examined and its enzymatic properties were investigated using several biochemical and biophysical methods. Interestingly, Ha HSL acted on a large variety of substrates including tertiary alcohol esters and fish oils. Additionally, this enzyme was highly tolerant to high concentrations of salt, detergents, and glycerol. Furthermore, immobilized Ha HSL retained its activity for up to six cycles of use. Homology modeling suggested that aromatic amino acids (Trp 23 , Tyr 74 , Phe 78 , Trp 83 , and Phe 245 ) in close proximity to the substrate-binding pocket were important for enzyme activity. Mutational analysis revealed that Tyr 74 played an important role in substrate specificity, thermostability, and enantioselectivity. In summary, the current study provides an invaluable insight into the novel cold-active Ha HSL from H. arcticus , which can be efficiently and sustainably used in a wide range of biotechnological applications.

Molecular Characterization of a Novel Cold-Active Hormone-Sensitive Lipase (HaHSL) from Halocynthiibacter Arcticus