Please use this identifier to cite or link to this item:
http://hdl.handle.net/11455/63352
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kuo, Chia-Hung | en_US |
dc.contributor.author | Chiang, Shu-Hua | en_US |
dc.contributor.author | Ju, Hen-Yi | en_US |
dc.contributor.author | Chen, Yu-Min | en_US |
dc.contributor.author | Liao, Ming-Yuan | en_US |
dc.contributor.author | Liu, Yung-Chuan | en_US |
dc.contributor.author | Shieh, Chwen-Jen | en_US |
dc.date | 2012-08 | zh_TW |
dc.date.accessioned | 2014-06-09T07:05:07Z | - |
dc.date.available | 2014-06-09T07:05:07Z | - |
dc.identifier.uri | http://hdl.handle.net/11455/63352 | - |
dc.description.abstract | 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. | en_US |
dc.language.iso | en_US | zh_TW |
dc.relation | J Sci Food Agric, Volume 92, Page(s) 2141–2147. | en_US |
dc.relation.uri | http://dx.doi.org/10.1002/jsfa.5599 | en_US |
dc.subject | lipase | en_US |
dc.subject | 2-phenylethyl acetate | en_US |
dc.subject | kinetics | en_US |
dc.subject | acetylation | en_US |
dc.subject | transesterification | en_US |
dc.title | Enzymatic synthesis of rose aromatic ester (2-phenylethyl acetate) by lipase | en_US |
dc.type | Journal Article | zh_TW |
dc.identifier.doi | 10.1002/jsfa.5599 | zh_TW |
dc.contributor.cataloger | Wei Chun Wang | en_US |
item.grantfulltext | none | - |
item.fulltext | no fulltext | - |
item.cerifentitytype | Publications | - |
item.languageiso639-1 | en_US | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.openairetype | Journal Article | - |
Appears in Collections: | 生物科技發展中心 |
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