A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst
Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used a...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Cavalcante, Francisco Thálysson Tavares [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022transfer abstract |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Basal PPARα inhibits bile acid metabolism adaptation in chronic cholestatic model induced by α-naphthylisothiocyanate - Hua, Huiying ELSEVIER, 2018, an international journal, New York, NY [u.a.] |
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| Übergeordnetes Werk: |
volume:187 ; year:2022 ; day:1 ; month:11 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.indcrop.2022.115450 |
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ELV058836802 |
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| 245 | 1 | 0 | |a A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst |
| 264 | 1 | |c 2022transfer abstract | |
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| 520 | |a Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... | ||
| 520 | |a Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... | ||
| 650 | 7 | |a Biolubricants |2 Elsevier | |
| 650 | 7 | |a Molecular dynamics |2 Elsevier | |
| 650 | 7 | |a Molecular docking |2 Elsevier | |
| 700 | 1 | |a da Fonseca, Aluisio Marques |4 oth | |
| 700 | 1 | |a Holanda Alexandre, Jeferson Yves Nunes |4 oth | |
| 700 | 1 | |a dos Santos, José C.S. |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Hua, Huiying ELSEVIER |t Basal PPARα inhibits bile acid metabolism adaptation in chronic cholestatic model induced by α-naphthylisothiocyanate |d 2018 |d an international journal |g New York, NY [u.a.] |w (DE-627)ELV001103067 |
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10.1016/j.indcrop.2022.115450 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001910.pica (DE-627)ELV058836802 (ELSEVIER)S0926-6690(22)00933-5 DE-627 ger DE-627 rakwb eng 570 540 610 VZ 44.39 bkl Cavalcante, Francisco Thálysson Tavares verfasserin aut A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants Elsevier Molecular dynamics Elsevier Molecular docking Elsevier da Fonseca, Aluisio Marques oth Holanda Alexandre, Jeferson Yves Nunes oth dos Santos, José C.S. oth Enthalten in Elsevier Hua, Huiying ELSEVIER Basal PPARα inhibits bile acid metabolism adaptation in chronic cholestatic model induced by α-naphthylisothiocyanate 2018 an international journal New York, NY [u.a.] (DE-627)ELV001103067 volume:187 year:2022 day:1 month:11 pages:0 https://doi.org/10.1016/j.indcrop.2022.115450 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-PHA 44.39 Toxikologie VZ AR 187 2022 1 1101 0 |
| spelling |
10.1016/j.indcrop.2022.115450 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001910.pica (DE-627)ELV058836802 (ELSEVIER)S0926-6690(22)00933-5 DE-627 ger DE-627 rakwb eng 570 540 610 VZ 44.39 bkl Cavalcante, Francisco Thálysson Tavares verfasserin aut A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants Elsevier Molecular dynamics Elsevier Molecular docking Elsevier da Fonseca, Aluisio Marques oth Holanda Alexandre, Jeferson Yves Nunes oth dos Santos, José C.S. oth Enthalten in Elsevier Hua, Huiying ELSEVIER Basal PPARα inhibits bile acid metabolism adaptation in chronic cholestatic model induced by α-naphthylisothiocyanate 2018 an international journal New York, NY [u.a.] (DE-627)ELV001103067 volume:187 year:2022 day:1 month:11 pages:0 https://doi.org/10.1016/j.indcrop.2022.115450 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-PHA 44.39 Toxikologie VZ AR 187 2022 1 1101 0 |
| allfields_unstemmed |
10.1016/j.indcrop.2022.115450 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001910.pica (DE-627)ELV058836802 (ELSEVIER)S0926-6690(22)00933-5 DE-627 ger DE-627 rakwb eng 570 540 610 VZ 44.39 bkl Cavalcante, Francisco Thálysson Tavares verfasserin aut A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants Elsevier Molecular dynamics Elsevier Molecular docking Elsevier da Fonseca, Aluisio Marques oth Holanda Alexandre, Jeferson Yves Nunes oth dos Santos, José C.S. oth Enthalten in Elsevier Hua, Huiying ELSEVIER Basal PPARα inhibits bile acid metabolism adaptation in chronic cholestatic model induced by α-naphthylisothiocyanate 2018 an international journal New York, NY [u.a.] (DE-627)ELV001103067 volume:187 year:2022 day:1 month:11 pages:0 https://doi.org/10.1016/j.indcrop.2022.115450 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-PHA 44.39 Toxikologie VZ AR 187 2022 1 1101 0 |
| allfieldsGer |
10.1016/j.indcrop.2022.115450 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001910.pica (DE-627)ELV058836802 (ELSEVIER)S0926-6690(22)00933-5 DE-627 ger DE-627 rakwb eng 570 540 610 VZ 44.39 bkl Cavalcante, Francisco Thálysson Tavares verfasserin aut A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants Elsevier Molecular dynamics Elsevier Molecular docking Elsevier da Fonseca, Aluisio Marques oth Holanda Alexandre, Jeferson Yves Nunes oth dos Santos, José C.S. oth Enthalten in Elsevier Hua, Huiying ELSEVIER Basal PPARα inhibits bile acid metabolism adaptation in chronic cholestatic model induced by α-naphthylisothiocyanate 2018 an international journal New York, NY [u.a.] (DE-627)ELV001103067 volume:187 year:2022 day:1 month:11 pages:0 https://doi.org/10.1016/j.indcrop.2022.115450 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-PHA 44.39 Toxikologie VZ AR 187 2022 1 1101 0 |
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10.1016/j.indcrop.2022.115450 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001910.pica (DE-627)ELV058836802 (ELSEVIER)S0926-6690(22)00933-5 DE-627 ger DE-627 rakwb eng 570 540 610 VZ 44.39 bkl Cavalcante, Francisco Thálysson Tavares verfasserin aut A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... Biolubricants Elsevier Molecular dynamics Elsevier Molecular docking Elsevier da Fonseca, Aluisio Marques oth Holanda Alexandre, Jeferson Yves Nunes oth dos Santos, José C.S. oth Enthalten in Elsevier Hua, Huiying ELSEVIER Basal PPARα inhibits bile acid metabolism adaptation in chronic cholestatic model induced by α-naphthylisothiocyanate 2018 an international journal New York, NY [u.a.] (DE-627)ELV001103067 volume:187 year:2022 day:1 month:11 pages:0 https://doi.org/10.1016/j.indcrop.2022.115450 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA SSG-OPC-PHA 44.39 Toxikologie VZ AR 187 2022 1 1101 0 |
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A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst |
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Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... |
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Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... |
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Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy... |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV058836802</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230626051711.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">221103s2022 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.indcrop.2022.115450</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">/cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001910.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV058836802</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0926-6690(22)00933-5</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="a">540</subfield><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">44.39</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Cavalcante, Francisco Thálysson Tavares</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">A stepwise docking and molecular dynamics approach for enzymatic biolubricant production using Lipase Eversa® Transform as a biocatalyst</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2022transfer abstract</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy...</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Biolubricants have gained a notable market share in the last decade due to the increased interest in replacing petroleum-based lubricants in various applications. Biolubricants are produced by using renewable raw materials such as vegetable oils, and enzymes such as lipases. The latter can be used as catalysts for biolubricant synthesis, which renders these processes environmentally friendly. Among the several innovations enabled by enzymatic engineering tools, the lipase Eversa® Transform 2.0 stands out as a genetically-modified and low-cost enzymatic formulation that has shown high activity in the production of biodiesel, fatty acids, and biolubricants. In addition to enzymatic engineering, advanced computational tools, such as docking and molecular dynamics, can also be powerful allies in the development of competitive products that impart low negative impact in the environment. These simulation tools enable the elucidation and understanding of reaction mechanisms, cut reagent costs, and inform choices regarding materials and conditions to be used in related industrial processes. Thus being, this work proposed the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0. Molecular dockings showed that the predominant interactions between the ligands and the amino acid residues that make up the active site of the enzyme and its surroundings were of Van der Waals and hydrophobic nature. Through simulations via molecular dynamics, it was found that these interactions were responsible for the stability of the lipase-ligand complex, given the low number of hydrogen bonds formed during the simulations. Furthermore, the low variation in the position of the lipase-ligand complexes comparatively to their initial conformations over the production stages attested that the chosen docking poses were adequate to describe the ligand conformations in the region of the active sites of the enzyme. These results also provide a structural view of the interactions between lipase Eversa® and the fatty esters used as lubricants, and confirm the potential in the use of these alcohols in this process. Finally, an in vitro validation showed improved results of esterification activity of the lipase with isoamyl alcohol. This hinted that the substrate that was in closer conformation and that showed shorter and more stable hydrogen bonds with the active sites of the enzy...</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Biolubricants</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Molecular dynamics</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Molecular docking</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">da Fonseca, Aluisio Marques</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Holanda Alexandre, Jeferson Yves Nunes</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">dos Santos, José C.S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Elsevier</subfield><subfield code="a">Hua, Huiying ELSEVIER</subfield><subfield code="t">Basal PPARα inhibits bile acid metabolism adaptation in chronic cholestatic model induced by α-naphthylisothiocyanate</subfield><subfield code="d">2018</subfield><subfield code="d">an international journal</subfield><subfield code="g">New York, NY [u.a.]</subfield><subfield code="w">(DE-627)ELV001103067</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:187</subfield><subfield code="g">year:2022</subfield><subfield code="g">day:1</subfield><subfield code="g">month:11</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.indcrop.2022.115450</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-PHA</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">44.39</subfield><subfield code="j">Toxikologie</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">187</subfield><subfield code="j">2022</subfield><subfield code="b">1</subfield><subfield code="c">1101</subfield><subfield code="h">0</subfield></datafield></record></collection>
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