Lipase – catalyzed formation of pentyl nonanoate using screened immobilized lipase from Rhizomucor meihei
Bio-catalysis has attracted the special attention of industrial flavour producers in the production of valuable ester compounds. In this study, the synthesis of pentyl nonanoate ester (a short chain ester with fruity aroma) was carried out with a commercial immobilized lipase from Rhizomucor meihei...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Brazilian Society of Chemical Engineering
2019
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| Online Access: | http://psasir.upm.edu.my/id/eprint/81235/1/Lipase.pdf |
| _version_ | 1825951407120842752 |
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| author | Muniandy, Megala Lasekan, Ola Mohd Ghazali, Hasanah Abdul Rahman, Mohd Basyaruddin |
| author_facet | Muniandy, Megala Lasekan, Ola Mohd Ghazali, Hasanah Abdul Rahman, Mohd Basyaruddin |
| author_sort | Muniandy, Megala |
| collection | UPM |
| description | Bio-catalysis has attracted the special attention of industrial flavour producers in the production of valuable ester compounds. In this study, the synthesis of pentyl nonanoate ester (a short chain ester with fruity aroma) was carried out with a commercial immobilized lipase from Rhizomucor meihei Lipozyme (RMIM) as biocatalyst in the esterification reaction between nonanoic acid and pentanol. Various reaction parameters such as enzyme concentration, substrate concentration, reaction temperature and reaction time in solvent-free system were screened to enhance the ester formation with the best yield. A maximum yield for pentyl nonanoate (86.08 %) in a solvent-free system was obtained within 150 min, at a reaction temperature of 45 OC, molar ratio of 1:9 M, amount of enzyme of 0.2 g, water addition of 0.2 % v/v and shaking speed of 150 rpm. This work suggests that pentyl nonanoate ester can be produced in a very high yield and in a short period by lipase-catalysed reactions of nonanoic acid and pentanol, using immobilized lipase from RMIM (lipase from Rhizomucor miehei immobilized on anionic exchange support). |
| first_indexed | 2024-03-06T10:29:33Z |
| format | Article |
| id | upm.eprints-81235 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T10:29:33Z |
| publishDate | 2019 |
| publisher | Brazilian Society of Chemical Engineering |
| record_format | dspace |
| spelling | upm.eprints-812352021-09-26T21:07:06Z http://psasir.upm.edu.my/id/eprint/81235/ Lipase – catalyzed formation of pentyl nonanoate using screened immobilized lipase from Rhizomucor meihei Muniandy, Megala Lasekan, Ola Mohd Ghazali, Hasanah Abdul Rahman, Mohd Basyaruddin Bio-catalysis has attracted the special attention of industrial flavour producers in the production of valuable ester compounds. In this study, the synthesis of pentyl nonanoate ester (a short chain ester with fruity aroma) was carried out with a commercial immobilized lipase from Rhizomucor meihei Lipozyme (RMIM) as biocatalyst in the esterification reaction between nonanoic acid and pentanol. Various reaction parameters such as enzyme concentration, substrate concentration, reaction temperature and reaction time in solvent-free system were screened to enhance the ester formation with the best yield. A maximum yield for pentyl nonanoate (86.08 %) in a solvent-free system was obtained within 150 min, at a reaction temperature of 45 OC, molar ratio of 1:9 M, amount of enzyme of 0.2 g, water addition of 0.2 % v/v and shaking speed of 150 rpm. This work suggests that pentyl nonanoate ester can be produced in a very high yield and in a short period by lipase-catalysed reactions of nonanoic acid and pentanol, using immobilized lipase from RMIM (lipase from Rhizomucor miehei immobilized on anionic exchange support). Brazilian Society of Chemical Engineering 2019-07 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/81235/1/Lipase.pdf Muniandy, Megala and Lasekan, Ola and Mohd Ghazali, Hasanah and Abdul Rahman, Mohd Basyaruddin (2019) Lipase – catalyzed formation of pentyl nonanoate using screened immobilized lipase from Rhizomucor meihei. Brazilian Journal of Chemical Engineering, 36 (3). pp. 1089-1097. ISSN 0104-6632: EISSN: 1678-4383 https://www.scielo.br/j/bjce/a/k6PkBtq4HnbtJpFzQmdvGtF/?lang=en https://doi.org/10.1590/0104-6632.20190363s20180419 |
| spellingShingle | Muniandy, Megala Lasekan, Ola Mohd Ghazali, Hasanah Abdul Rahman, Mohd Basyaruddin Lipase – catalyzed formation of pentyl nonanoate using screened immobilized lipase from Rhizomucor meihei |
| title | Lipase – catalyzed formation of pentyl nonanoate using screened immobilized lipase from Rhizomucor meihei |
| title_full | Lipase – catalyzed formation of pentyl nonanoate using screened immobilized lipase from Rhizomucor meihei |
| title_fullStr | Lipase – catalyzed formation of pentyl nonanoate using screened immobilized lipase from Rhizomucor meihei |
| title_full_unstemmed | Lipase – catalyzed formation of pentyl nonanoate using screened immobilized lipase from Rhizomucor meihei |
| title_short | Lipase – catalyzed formation of pentyl nonanoate using screened immobilized lipase from Rhizomucor meihei |
| title_sort | lipase catalyzed formation of pentyl nonanoate using screened immobilized lipase from rhizomucor meihei |
| url | http://psasir.upm.edu.my/id/eprint/81235/1/Lipase.pdf |
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