Effects of alcohol concentration and temperature on the dynamics and stability of mutant Staphylococcal lipase
The stability and activity of lipase in organic media are important parameters in determining how quickly biocatalysis proceeds. This study aimed to examine the effects of two commonly used alcohols in industrial applications, methanol (MtOH) and ethanol (EtOH) on the conformational stability and ca...
| Main Authors: | , , , , , |
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| Format: | Article |
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Informa UK Limited
2023
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| Online Access: | http://psasir.upm.edu.my/id/eprint/107559/ |
| _version_ | 1848864929331806208 |
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| author | Ong, Shir Nee Ahmad Kamarudin, Nor Hafizah Mohd Shariff, Fairolniza Muhd Noor, Noor Dina Mohamad Ali, Mohd Shukuri Raja Abd. Rahman, Raja Noor Zaliha |
| author_facet | Ong, Shir Nee Ahmad Kamarudin, Nor Hafizah Mohd Shariff, Fairolniza Muhd Noor, Noor Dina Mohamad Ali, Mohd Shukuri Raja Abd. Rahman, Raja Noor Zaliha |
| author_sort | Ong, Shir Nee |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | The stability and activity of lipase in organic media are important parameters in determining how quickly biocatalysis proceeds. This study aimed to examine the effects of two commonly used alcohols in industrial applications, methanol (MtOH) and ethanol (EtOH) on the conformational stability and catalytic activity of G210C lipase, a laboratory-evolved mutant of Staphylococcus epidermidis AT2 lipase. Simulation studies were performed using an open-form predicted structure under 30, 40 and 50 of MtOH and EtOH at 25‰°C and 45‰°C. The overall enzyme structure becomes more flexible with increasing concentration of MtOH and exhibited the highest flexibility in 40 EtOH. In EtOH, the movement of the lid was found to be temperature-dependent with a noticeable shift in the lid position at 45‰°C. Lid opening was evidenced at 50 of MtOH and EtOH which was supported by the increase in SASA of hydrophobic residues of the lid and catalytic triad. The active site remained mostly intact. An open-closed lid transition was observed when the structure was re-simulated in water. Experimental evaluation of the lipase stability showed that the half-life reduced when the enzyme was treated with 40 (v/v) and 50 (v/v) of EtOH and MtOH respectively. The finding implies that a high concentration of alcohol and elevated temperature can induce the lid opening of lipase which could be essential for the activation of the enzyme, provided that the catalytic performance in the active site is not compromised. |
| first_indexed | 2025-11-15T13:56:37Z |
| format | Article |
| id | upm-107559 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T13:56:37Z |
| publishDate | 2023 |
| publisher | Informa UK Limited |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1075592024-07-24T08:41:08Z http://psasir.upm.edu.my/id/eprint/107559/ Effects of alcohol concentration and temperature on the dynamics and stability of mutant Staphylococcal lipase Ong, Shir Nee Ahmad Kamarudin, Nor Hafizah Mohd Shariff, Fairolniza Muhd Noor, Noor Dina Mohamad Ali, Mohd Shukuri Raja Abd. Rahman, Raja Noor Zaliha The stability and activity of lipase in organic media are important parameters in determining how quickly biocatalysis proceeds. This study aimed to examine the effects of two commonly used alcohols in industrial applications, methanol (MtOH) and ethanol (EtOH) on the conformational stability and catalytic activity of G210C lipase, a laboratory-evolved mutant of Staphylococcus epidermidis AT2 lipase. Simulation studies were performed using an open-form predicted structure under 30, 40 and 50 of MtOH and EtOH at 25‰°C and 45‰°C. The overall enzyme structure becomes more flexible with increasing concentration of MtOH and exhibited the highest flexibility in 40 EtOH. In EtOH, the movement of the lid was found to be temperature-dependent with a noticeable shift in the lid position at 45‰°C. Lid opening was evidenced at 50 of MtOH and EtOH which was supported by the increase in SASA of hydrophobic residues of the lid and catalytic triad. The active site remained mostly intact. An open-closed lid transition was observed when the structure was re-simulated in water. Experimental evaluation of the lipase stability showed that the half-life reduced when the enzyme was treated with 40 (v/v) and 50 (v/v) of EtOH and MtOH respectively. The finding implies that a high concentration of alcohol and elevated temperature can induce the lid opening of lipase which could be essential for the activation of the enzyme, provided that the catalytic performance in the active site is not compromised. Informa UK Limited 2023-11-15 Article PeerReviewed Ong, Shir Nee and Ahmad Kamarudin, Nor Hafizah and Mohd Shariff, Fairolniza and Muhd Noor, Noor Dina and Mohamad Ali, Mohd Shukuri and Raja Abd. Rahman, Raja Noor Zaliha (2023) Effects of alcohol concentration and temperature on the dynamics and stability of mutant Staphylococcal lipase. Journal of Biomolecular Structure and Dynamics. pp. 1-17. ISSN 0739-1102; ESSN: 1538-0254 https://www.tandfonline.com/doi/full/10.1080/07391102.2023.2282177 10.1080/07391102.2023.2282177 |
| spellingShingle | Ong, Shir Nee Ahmad Kamarudin, Nor Hafizah Mohd Shariff, Fairolniza Muhd Noor, Noor Dina Mohamad Ali, Mohd Shukuri Raja Abd. Rahman, Raja Noor Zaliha Effects of alcohol concentration and temperature on the dynamics and stability of mutant Staphylococcal lipase |
| title | Effects of alcohol concentration and temperature on the dynamics and stability of mutant Staphylococcal lipase |
| title_full | Effects of alcohol concentration and temperature on the dynamics and stability of mutant Staphylococcal lipase |
| title_fullStr | Effects of alcohol concentration and temperature on the dynamics and stability of mutant Staphylococcal lipase |
| title_full_unstemmed | Effects of alcohol concentration and temperature on the dynamics and stability of mutant Staphylococcal lipase |
| title_short | Effects of alcohol concentration and temperature on the dynamics and stability of mutant Staphylococcal lipase |
| title_sort | effects of alcohol concentration and temperature on the dynamics and stability of mutant staphylococcal lipase |
| url | http://psasir.upm.edu.my/id/eprint/107559/ http://psasir.upm.edu.my/id/eprint/107559/ http://psasir.upm.edu.my/id/eprint/107559/ |