Immobilized Lipase Catalysed Esterification Of Formic Acid And Methanol
Methyl formate is the simplest ester with various uses in industrial applications. Fischer esterification is a conventional esterification that uses acid catalysts, giving drawbacks such as environmental issues. The utilization of biocatalyst is an alternative method for esterification reaction, whi...
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| Format: | Monograph |
| Language: | English |
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Universiti Sains Malaysia
2022
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| Online Access: | http://eprints.usm.my/55413/ http://eprints.usm.my/55413/1/Immobilized%20Lipase%20Catalysed%20Esterification%20Of%20Formic%20Acid%20And%20Methanol.pdf |
| _version_ | 1848883073425342464 |
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| author | Ali, Maisara Adleena Mohd |
| author_facet | Ali, Maisara Adleena Mohd |
| author_sort | Ali, Maisara Adleena Mohd |
| building | USM Institutional Repository |
| collection | Online Access |
| description | Methyl formate is the simplest ester with various uses in industrial applications. Fischer esterification is a conventional esterification that uses acid catalysts, giving drawbacks such as environmental issues. The utilization of biocatalyst is an alternative method for esterification reaction, which provides better sustainability and eco-friendly aspect. This thesis describes the optimization of enzymatic esterification by using the OFAT technique. The reaction of enzymatic esterification involved formic acid and methanol catalyzed by immobilized Candida rugosa lipase in n-hexane solvent to produce methyl formate. 62.24 U/mg of free C. rugosa lipase was immobilized by physical adsorption on Celite 545 support, which resulted in 50 U/mg support in a specific activity. The effect of reaction time, enzyme loading and substrate molar ratio were studied. The highest conversion of 30.22% was obtained at 40°C, with a 1:4 molar ratio of formic acid to methanol, 4 g/L of enzyme loading with an agitation speed of 150 rpm in 1.5mL n-hexane for 60 minutes reaction. Secondary data from the research article was used to study and compare the kinetic model via non-linear regression analysis through rate equation. The best fit with the experimental data was Ping Pong Bi-Bi with inhibition by both substrates with an R2 value of 0.98. The kinetic parameter obtained were, Vmax= 5.98 mmol/min/g, KmM = 0.24 mmol, KmO = 1.16 mmol, KiO = 0.68 mmol and KiM = 0.19 mmol. |
| first_indexed | 2025-11-15T18:45:01Z |
| format | Monograph |
| id | usm-55413 |
| institution | Universiti Sains Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T18:45:01Z |
| publishDate | 2022 |
| publisher | Universiti Sains Malaysia |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | usm-554132022-10-25T07:35:24Z http://eprints.usm.my/55413/ Immobilized Lipase Catalysed Esterification Of Formic Acid And Methanol Ali, Maisara Adleena Mohd T Technology TP155-156 Chemical engineering Methyl formate is the simplest ester with various uses in industrial applications. Fischer esterification is a conventional esterification that uses acid catalysts, giving drawbacks such as environmental issues. The utilization of biocatalyst is an alternative method for esterification reaction, which provides better sustainability and eco-friendly aspect. This thesis describes the optimization of enzymatic esterification by using the OFAT technique. The reaction of enzymatic esterification involved formic acid and methanol catalyzed by immobilized Candida rugosa lipase in n-hexane solvent to produce methyl formate. 62.24 U/mg of free C. rugosa lipase was immobilized by physical adsorption on Celite 545 support, which resulted in 50 U/mg support in a specific activity. The effect of reaction time, enzyme loading and substrate molar ratio were studied. The highest conversion of 30.22% was obtained at 40°C, with a 1:4 molar ratio of formic acid to methanol, 4 g/L of enzyme loading with an agitation speed of 150 rpm in 1.5mL n-hexane for 60 minutes reaction. Secondary data from the research article was used to study and compare the kinetic model via non-linear regression analysis through rate equation. The best fit with the experimental data was Ping Pong Bi-Bi with inhibition by both substrates with an R2 value of 0.98. The kinetic parameter obtained were, Vmax= 5.98 mmol/min/g, KmM = 0.24 mmol, KmO = 1.16 mmol, KiO = 0.68 mmol and KiM = 0.19 mmol. Universiti Sains Malaysia 2022-07-01 Monograph NonPeerReviewed application/pdf en http://eprints.usm.my/55413/1/Immobilized%20Lipase%20Catalysed%20Esterification%20Of%20Formic%20Acid%20And%20Methanol.pdf Ali, Maisara Adleena Mohd (2022) Immobilized Lipase Catalysed Esterification Of Formic Acid And Methanol. Project Report. Universiti Sains Malaysia, Pusat Pengajian Kejuruteraan Kimia. (Submitted) |
| spellingShingle | T Technology TP155-156 Chemical engineering Ali, Maisara Adleena Mohd Immobilized Lipase Catalysed Esterification Of Formic Acid And Methanol |
| title | Immobilized Lipase Catalysed Esterification Of Formic Acid And Methanol |
| title_full | Immobilized Lipase Catalysed Esterification Of Formic Acid And Methanol |
| title_fullStr | Immobilized Lipase Catalysed Esterification Of Formic Acid And Methanol |
| title_full_unstemmed | Immobilized Lipase Catalysed Esterification Of Formic Acid And Methanol |
| title_short | Immobilized Lipase Catalysed Esterification Of Formic Acid And Methanol |
| title_sort | immobilized lipase catalysed esterification of formic acid and methanol |
| topic | T Technology TP155-156 Chemical engineering |
| url | http://eprints.usm.my/55413/ http://eprints.usm.my/55413/1/Immobilized%20Lipase%20Catalysed%20Esterification%20Of%20Formic%20Acid%20And%20Methanol.pdf |