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...

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Published in:Journal of the Science of Food and Agriculture
Main Authors: Kuo, Chia-Hung, Chiang, Shu-Hua, Ju, Hen-Yi, Chen, Yu-Min, Liao, Ming-Yuan, Liu, Yung-Chuan, Shieh, Chwen-Jen
Other Authors: Wei Chun Wang
Format: Article in Journal/Newspaper
Language:English
Published: 2012
Subjects:
Online Access:http://hdl.handle.net/11455/63352
https://doi.org/10.1002/jsfa.5599
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spelling ftnchunghsing:oai:ir.lib.nchu.edu.tw:11455/63352 2023-05-15T14:01:41+02:00 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 National Chung Hsing University Institutional Repository - NCHUIR Journal of the Science of Food and Agriculture 92 10 2141 2147
institution Open Polar
collection National Chung Hsing University Institutional Repository - NCHUIR
op_collection_id ftnchunghsing
language English
topic lipase
2-phenylethyl acetate
kinetics
acetylation
transesterification
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
topic_facet lipase
2-phenylethyl acetate
kinetics
acetylation
transesterification
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.
author2 Wei Chun Wang
format Article in Journal/Newspaper
author Kuo, Chia-Hung
Chiang, Shu-Hua
Ju, Hen-Yi
Chen, Yu-Min
Liao, Ming-Yuan
Liu, Yung-Chuan
Shieh, Chwen-Jen
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
title 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_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_sort enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase
publishDate 2012
url http://hdl.handle.net/11455/63352
https://doi.org/10.1002/jsfa.5599
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
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
op_doi https://doi.org/10.1002/jsfa.5599
container_title Journal of the Science of Food and Agriculture
container_volume 92
container_issue 10
container_start_page 2141
op_container_end_page 2147
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