Research Article Open Access

The Effect of NaCl on the Stability of Ab3 Lipase from Sphingobacterium sp. that Co-Expressed with LEA K Using In silico Approach

Ibrahim Muhammad1,2,3, Ng Siau Ning4, Nurul Izza Ismail1, Hasni Arsad5, Shinya Ikeno6 and Rashidah Abdul Rahim1,7
  • 1 School of Biological Sciences, University Sains Malaysia, Penang, Malaysia
  • 2 Petroleum Technology Development Fund (PTDF), Central Business District, 900001 Garki Abuja, Nigeria
  • 3 Department of Science Lab. Technology, Ramat Polytechnic Maiduguri, 600211 Borno, Nigeria
  • 4 School of Biological Sciences, University Sains Malaysia, Malaysia
  • 5 Advanced Medical and Dental Institute, University Sains Malaysia, Bandar Putra Bertam, Kepala Batas, Penang, Malaysia
  • 6 Department of Biological Functions and Engineering, Graduate School of Life Science and System Engineering, Kyushu Institute of Technology, Japan
  • 7 Centre for Chemical Biology (CCB@USM), Persiaran Bukit Jambul, Bayan Lepas, Penang, Malaysia

Abstract

This study explores how sodium chloride (NaCl) influences the binding affinity and stability of the Ab3 lipase-LEA K complex when interacting with olive oil, using molecular docking techniques. The docking simulations, conducted with AutoDock Vina, reveal that the presence of NaCl significantly enhances the binding affinity of the enzyme-substrate complex, increasing it from-6.55 kcal/mol in the absence of salt to-7.81 kcal/mol with salt. This improvement in binding affinity is accompanied by the formation of additional hydrogen bonds and hydrophobic interactions, indicating that NaCl induces a favourable conformational change in the enzyme complex. Notably, NaCl facilitates interaction with His287, a key residue in the catalytic triad, suggesting improved accessibility and orientation of the active site, which is crucial for catalytic efficiency. These findings underscore the role of NaCl in stabilizing the enzyme complex and enhancing its structural integrity and activity, which has significant implications for industrial applications. Specifically, in industries where processes occur under high-salt conditions, such as food processing and biofuel production, the ability of NaCl to enhance lipase stability and performance could lead to more efficient and cost-effective operations, reducing the need for frequent enzyme replacement and improving overall process efficiency.

American Journal of Biochemistry and Biotechnology
Volume 21 No. 1, 2025, 60-67

DOI: https://doi.org/10.3844/ajbbsp.2025.60.67

Submitted On: 4 September 2024 Published On: 9 March 2025

How to Cite: Muhammad, I., Ning, N. S., Ismail, N. I., Arsad, H., Ikeno, S. & Rahim, R. A. (2025). The Effect of NaCl on the Stability of Ab3 Lipase from Sphingobacterium sp. that Co-Expressed with LEA K Using In silico Approach. American Journal of Biochemistry and Biotechnology, 21(1), 60-67. https://doi.org/10.3844/ajbbsp.2025.60.67

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Keywords

  • Sodium Chloride
  • Ab3 Lipase-LEA K-Complex
  • Binding Affinity
  • Enzyme Stability
  • Catalytic Triad
  • Hydrogen Bonds
  • Hydrophobic Interactions
  • High-Salt Environments