Enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase
BACKGROUND: 2-Phenylethyl acetate (2-PEAc) is a highly valued natural volatile ester with a rose-like odour that is widely used to add scent or flavour to cosmetics, soaps, foods and drinks. In this study, 2-PEAc was synthesised enzymatically by transesterification of vinyl acetate with 2-phenethyl...
Published in: | Journal of the Science of Food and Agriculture |
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Main Authors: | , , , , , , |
Other Authors: | |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2012
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Subjects: | |
Online Access: | http://hdl.handle.net/11455/63352 https://doi.org/10.1002/jsfa.5599 |
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author | Kuo, Chia-Hung Chiang, Shu-Hua Ju, Hen-Yi Chen, Yu-Min Liao, Ming-Yuan Liu, Yung-Chuan Shieh, Chwen-Jen |
author2 | Wei Chun Wang |
author_facet | Kuo, Chia-Hung Chiang, Shu-Hua Ju, Hen-Yi Chen, Yu-Min Liao, Ming-Yuan Liu, Yung-Chuan Shieh, Chwen-Jen |
author_sort | Kuo, Chia-Hung |
collection | Unknown |
container_issue | 10 |
container_start_page | 2141 |
container_title | Journal of the Science of Food and Agriculture |
container_volume | 92 |
description | BACKGROUND: 2-Phenylethyl acetate (2-PEAc) is a highly valued natural volatile ester with a rose-like odour that is widely used to add scent or flavour to cosmetics, soaps, foods and drinks. In this study, 2-PEAc was synthesised enzymatically by transesterification of vinyl acetate with 2-phenethyl alcohol catalysed by immobilised lipase (Novozym 435) from Candida antarctica. RESULTS: Response surface methodology and a three-level/three-factor Box–Behnken design were used to evaluate the effects of time, temperature and enzyme amount on the molar conversion % of 2-PEAc. The results showed that temperature was the most important variable. Based on the ridge max analysis results, optimum enzymatic synthesis conditions were predicted as a reaction time of 79 min, a temperature of 57.8 ◦C and an enzyme amount of 122.5 mg. The predicted and experimental yields were 86.4 and 85.4% respectively. CONCLUSION: Three immobilised lipases were screened and 15 reaction conditions were tested in order to find the combination for maximum yield. The optimisation of 2-PEAc synthesis catalysed by Novozym 435 was successfully developed. The kinetic study of this transesterification reaction showed that it followed an ordered ping-pong bi-bimechanism without any inhibition by reactants. |
format | Article in Journal/Newspaper |
genre | Antarc* Antarctica |
genre_facet | Antarc* Antarctica |
id | ftnchunghsing:oai:ir.lib.nchu.edu.tw:11455/63352 |
institution | Open Polar |
language | English |
op_collection_id | ftnchunghsing |
op_container_end_page | 2147 |
op_doi | https://doi.org/10.1002/jsfa.5599 |
op_relation | #PLACEHOLDER_PARENT_METADATA_VALUE# J Sci Food Agric, Volume 92, Page(s) 2141–2147. http://dx.doi.org/10.1002/jsfa.5599 http://hdl.handle.net/11455/63352 doi:10.1002/jsfa.5599 |
op_rights | none |
publishDate | 2012 |
record_format | openpolar |
spelling | ftnchunghsing:oai:ir.lib.nchu.edu.tw:11455/63352 2025-01-16T19:24:25+00:00 Enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase Kuo, Chia-Hung Chiang, Shu-Hua Ju, Hen-Yi Chen, Yu-Min Liao, Ming-Yuan Liu, Yung-Chuan Shieh, Chwen-Jen Wei Chun Wang 2012-08 http://hdl.handle.net/11455/63352 https://doi.org/10.1002/jsfa.5599 en_US eng #PLACEHOLDER_PARENT_METADATA_VALUE# J Sci Food Agric, Volume 92, Page(s) 2141–2147. http://dx.doi.org/10.1002/jsfa.5599 http://hdl.handle.net/11455/63352 doi:10.1002/jsfa.5599 none lipase 2-phenylethyl acetate kinetics acetylation transesterification Journal Article 2012 ftnchunghsing https://doi.org/10.1002/jsfa.5599 2021-06-26T20:37:21Z BACKGROUND: 2-Phenylethyl acetate (2-PEAc) is a highly valued natural volatile ester with a rose-like odour that is widely used to add scent or flavour to cosmetics, soaps, foods and drinks. In this study, 2-PEAc was synthesised enzymatically by transesterification of vinyl acetate with 2-phenethyl alcohol catalysed by immobilised lipase (Novozym 435) from Candida antarctica. RESULTS: Response surface methodology and a three-level/three-factor Box–Behnken design were used to evaluate the effects of time, temperature and enzyme amount on the molar conversion % of 2-PEAc. The results showed that temperature was the most important variable. Based on the ridge max analysis results, optimum enzymatic synthesis conditions were predicted as a reaction time of 79 min, a temperature of 57.8 ◦C and an enzyme amount of 122.5 mg. The predicted and experimental yields were 86.4 and 85.4% respectively. CONCLUSION: Three immobilised lipases were screened and 15 reaction conditions were tested in order to find the combination for maximum yield. The optimisation of 2-PEAc synthesis catalysed by Novozym 435 was successfully developed. The kinetic study of this transesterification reaction showed that it followed an ordered ping-pong bi-bimechanism without any inhibition by reactants. Article in Journal/Newspaper Antarc* Antarctica Unknown Journal of the Science of Food and Agriculture 92 10 2141 2147 |
spellingShingle | lipase 2-phenylethyl acetate kinetics acetylation transesterification Kuo, Chia-Hung Chiang, Shu-Hua Ju, Hen-Yi Chen, Yu-Min Liao, Ming-Yuan Liu, Yung-Chuan Shieh, Chwen-Jen Enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase |
title | Enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase |
title_full | Enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase |
title_fullStr | Enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase |
title_full_unstemmed | Enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase |
title_short | Enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase |
title_sort | enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase |
topic | lipase 2-phenylethyl acetate kinetics acetylation transesterification |
topic_facet | lipase 2-phenylethyl acetate kinetics acetylation transesterification |
url | http://hdl.handle.net/11455/63352 https://doi.org/10.1002/jsfa.5599 |