Yarrowia lipolytica is recognized as a promising host for heterologous protein production due to its high secretion capacity. Among its enzymes, lipase plays a crucial role in diverse industrial applications, including detergent, food, cosmetic, pharmaceutical, and environmental sectors. Lip2, the only extracellular lipase of Y. lipolytica, is a glycosylated enzyme composed of 301 amino acids and several disulfide bonds. Its crystal structure reveals two N-glycosylation sites located at N113 and N134. Lip2 exhibits catalytic activity at low temperatures (around 5 °C), shows optimal performance at 37 °C, and rapidly loses activity above 50 °C. To explore the influence of sugar moieties on the thermodynamic stability of Lip2, the complete glycosylated structure was examined through molecular dynamics (MD) simulations. The simulations were carried out using GROMACS 5.1.4 with the CHARMM36M force field at three functional temperatures (300 K, 310 K, and 333 K) for a total production run of 40 ns. The results demonstrated that the glycosylated Lip2 exhibited higher temperature-dependent structural fluctuations, while the deglycosylated form showed enhanced thermostability upon temperature increase. Further analysis revealed that glycosylation affects not only the residues adjacent to the glycosylation sites but also induces conformational changes in distant regions of the protein. This leads to increased residue flexibility and a higher radius of gyration, which was supported by root-mean-square deviation (RMSD) analysis. Additionally, hydrogen bond analysis indicated that the non-glycosylated form maintained a higher number and longer lifetimes of hydrogen bonds across all temperatures, suggesting a more stable folding pattern. In conclusion, the overall stability of the glycosylated Lip2 decreases compared to its non-glycosylated counterpart, potentially due to complex molecular interactions. This in silico study provides new insights into the thermodynamic behavior of Lip2 in aqueous environments and establishes a foundation for future studies on the independent effects of glucosamine groups on enzyme stability.
Esmaeili shaikhabad,Samaneh . (1404). In silico study on the effects of Glucosamine group on Thermal Stability of Yarrowia lipolytica Lip2 lipase. انفورماتیک در زیست شناسی، بهداشت و غذا, 2(2), 120-131. doi: 10.22034/ibhf.2025.559174.1046
MLA
Esmaeili shaikhabad,Samaneh . "In silico study on the effects of Glucosamine group on Thermal Stability of Yarrowia lipolytica Lip2 lipase", انفورماتیک در زیست شناسی، بهداشت و غذا, 2, 2, 1404, 120-131. doi: 10.22034/ibhf.2025.559174.1046
HARVARD
Esmaeili shaikhabad Samaneh. (1404). 'In silico study on the effects of Glucosamine group on Thermal Stability of Yarrowia lipolytica Lip2 lipase', انفورماتیک در زیست شناسی، بهداشت و غذا, 2(2), pp. 120-131. doi: 10.22034/ibhf.2025.559174.1046
CHICAGO
Samaneh Esmaeili shaikhabad, "In silico study on the effects of Glucosamine group on Thermal Stability of Yarrowia lipolytica Lip2 lipase," انفورماتیک در زیست شناسی، بهداشت و غذا, 2 2 (1404): 120-131, doi: 10.22034/ibhf.2025.559174.1046
VANCOUVER
Esmaeili shaikhabad Samaneh. In silico study on the effects of Glucosamine group on Thermal Stability of Yarrowia lipolytica Lip2 lipase. انفورماتیک در زیست شناسی، بهداشت و غذا, 1404; 2(2): 120-131. doi: 10.22034/ibhf.2025.559174.1046
