PRODUCTION OF EUGENYL ACETATE FROM CLOVE BUD OIL USING IMMOBILIZED CANDIDA RUGOSA LIPASE ENZYME
Eugenyl acetate (EA) is often found in fragrances and flavors in food as an alternative to eugenol which is prohibited at certain levels related to food safety. EA has antibacterial and anti-toxic properties that are actively able to control pest outbreaks and is an anticarcinogenic compound that ca...
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id-itb.:874382025-01-30T08:24:37ZPRODUCTION OF EUGENYL ACETATE FROM CLOVE BUD OIL USING IMMOBILIZED CANDIDA RUGOSA LIPASE ENZYME X. Gani Susanto, F. Indonesia Theses Clove, eugenol, eugenyl acetate, esterification, lipase INSTITUT TEKNOLOGI BANDUNG https://digilib.itb.ac.id/gdl/view/87438 Eugenyl acetate (EA) is often found in fragrances and flavors in food as an alternative to eugenol which is prohibited at certain levels related to food safety. EA has antibacterial and anti-toxic properties that are actively able to control pest outbreaks and is an anticarcinogenic compound that can prevent cancer growth, as well as an antimicrobial compound. EA can be found naturally in essential oils but in small amounts, for example in clove oil only around 7-9%. Efforts to develop more environmentally friendly EA production methods on an industrial scale must be explored further. Bringing research on EA synthesis to a new chapter-through enzymatic methods that still require exploration of newer things to enrich feasible alternative technologies to be applied to an industrial scale-not just stopping at the laboratory scale. This research was started to explore the enzymatic synthesis of EA, which aims for a more sustainable and environmentally friendly approach-saving water usage, avoiding waste production that pollutes the environment, and meeting natural aspects that meet food safety standards. Lipase enzyme immobilized on clinoptilolite was selected as the catalyst showing an outstanding adsorption efficiency of 98.1% and peak activity at 45 °C and pH 7. Immobilization provided benefits such as improved stability and reduced cost through reusability over four cycles, with the immobilized enzyme retaining 66.67% residual activity after 6 h compared to the soluble enzyme at 6.20%. The synthesis of EA involved the esterification reaction of eugenol for 6 h, at a molar ratio of eugenol to acetic anhydride of 1:3, a temperature of 30 °C to 60 °C, an enzyme concentration of 5% by weight of eugenol, and agitation at 150 rpm. The optimum condition, resulting in a eugenol conversion of 90.12%, was found at 45 °C. Purity analysis via GC-FID confirmed the quality of EA at 48.9%. Kinetic parameters were studied using Lineweaver-Burk plots with the Ping Pong Bi Bi mechanism equation which has an R2 value of 0.99-giving kma, kmB, and Vmax of 0.88, 21.20, and 26.24, respectively. This enzymatic approach unlocks the potential of eugenyl acetate and overcomes the environmental and operational challenges associated with traditional methods. text |
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Eugenyl acetate (EA) is often found in fragrances and flavors in food as an alternative to eugenol which is prohibited at certain levels related to food safety. EA has antibacterial and anti-toxic properties that are actively able to control pest outbreaks and is an anticarcinogenic compound that can prevent cancer growth, as well as an antimicrobial compound. EA can be found naturally in essential oils but in small amounts, for example in clove oil only around 7-9%. Efforts to develop more environmentally friendly EA production methods on an industrial scale must be explored further. Bringing research on EA synthesis to a new chapter-through enzymatic methods that still require exploration of newer things to enrich feasible alternative technologies to be applied to an industrial scale-not just stopping at the laboratory scale.
This research was started to explore the enzymatic synthesis of EA, which aims for a more sustainable and environmentally friendly approach-saving water usage, avoiding waste production that pollutes the environment, and meeting natural aspects that meet food safety standards. Lipase enzyme immobilized on clinoptilolite was selected as the catalyst showing an outstanding adsorption efficiency of 98.1% and peak activity at 45 °C and pH 7. Immobilization provided benefits such as improved stability and reduced cost through reusability over four cycles, with the immobilized enzyme retaining 66.67% residual activity after 6 h compared to the soluble enzyme at 6.20%.
The synthesis of EA involved the esterification reaction of eugenol for 6 h, at a molar ratio of eugenol to acetic anhydride of 1:3, a temperature of 30 °C to 60 °C, an enzyme concentration of 5% by weight of eugenol, and agitation at 150 rpm. The optimum condition, resulting in a eugenol conversion of 90.12%, was found at 45 °C. Purity analysis via GC-FID confirmed the quality of EA at 48.9%. Kinetic parameters were studied using Lineweaver-Burk plots with the Ping Pong Bi Bi mechanism equation which has an R2 value of 0.99-giving kma, kmB, and Vmax of 0.88, 21.20, and 26.24, respectively. This enzymatic approach unlocks the potential of eugenyl acetate and overcomes the environmental and operational challenges associated with traditional methods. |
format |
Theses |
author |
X. Gani Susanto, F. |
spellingShingle |
X. Gani Susanto, F. PRODUCTION OF EUGENYL ACETATE FROM CLOVE BUD OIL USING IMMOBILIZED CANDIDA RUGOSA LIPASE ENZYME |
author_facet |
X. Gani Susanto, F. |
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X. Gani Susanto, F. |
title |
PRODUCTION OF EUGENYL ACETATE FROM CLOVE BUD OIL USING IMMOBILIZED CANDIDA RUGOSA LIPASE ENZYME |
title_short |
PRODUCTION OF EUGENYL ACETATE FROM CLOVE BUD OIL USING IMMOBILIZED CANDIDA RUGOSA LIPASE ENZYME |
title_full |
PRODUCTION OF EUGENYL ACETATE FROM CLOVE BUD OIL USING IMMOBILIZED CANDIDA RUGOSA LIPASE ENZYME |
title_fullStr |
PRODUCTION OF EUGENYL ACETATE FROM CLOVE BUD OIL USING IMMOBILIZED CANDIDA RUGOSA LIPASE ENZYME |
title_full_unstemmed |
PRODUCTION OF EUGENYL ACETATE FROM CLOVE BUD OIL USING IMMOBILIZED CANDIDA RUGOSA LIPASE ENZYME |
title_sort |
production of eugenyl acetate from clove bud oil using immobilized candida rugosa lipase enzyme |
url |
https://digilib.itb.ac.id/gdl/view/87438 |
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