Enzymatic synthesis of rose aromatic ester (2‐phenylethyl acetate) by lipase

Kuo, Chia‐Hung; Chiang, Shu-Hua; Ju, Hen-Yi; Chen, Yumin; Liao, Ming-Yuan; Liu, Yung-Chuan; Shieh, Chwen‐Jen

doi:10.1002/jsfa.5599

Cited by 32 publications

(27 citation statements)

References 30 publications

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“…Several enzymatic methods have been reported for the preparation of 2-PEAc by lipase (Kuo, Liu, Chen, Chang, & Shieh, 2013;Kuo et al, 2012). However, there are some drawbacks by using enzymes in bioprocesses such as the need of long and complicated steps for enzyme isolation and purification.…”

Section: Discussionmentioning

confidence: 99%

Metabolic engineering of Escherichia coli for production of 2‐Phenylethylacetate from L‐phenylalanine

et al. 2017

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In order to meet the need of consumer preferences for natural flavor compounds, microbial synthesis method has become a very attractive alternative to the chemical production. The 2‐phenylethanol (2‐PE) and its ester 2‐phenylethylacetate (2‐PEAc) are two extremely important flavor compounds with a rose‐like odor. In recent years, Escherichia coli and yeast have been metabolically engineered to produce 2‐PE. However, a metabolic engineering approach for 2‐PEAc production is rare. Here, we designed and expressed a 2‐PEAc biosynthetic pathway in E. coli. This pathway comprised four steps: aminotransferase (ARO8) for transamination of L‐phenylalanine to phenylpyruvate, 2‐keto acid decarboxylase KDC for the decarboxylation of the phenylpyruvate to phenylacetaldehyde, aldehyde reductase YjgB for the reduction of phenylacetaldehyde to 2‐PE, alcohol acetyltransferase ATF1 for the esterification of 2‐PE to 2‐PEAc. Using the engineered E. coli strain for shake flasks cultivation with 1 g/L L‐phenylalanine, we achieved co‐production of 268 mg/L 2‐PEAc and 277 mg/L 2‐PE. Our results suggest that approximately 65% of L‐phenylalanine was utilized toward 2‐PEAc and 2‐PE biosynthesis and thus demonstrate potential industrial applicability of this microbial platform.

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Section: Discussionmentioning

confidence: 99%

Metabolic engineering of Escherichia coli for production of 2‐Phenylethylacetate from L‐phenylalanine

et al. 2017

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“…The temperature would also be considered important in the production of ester since its increase would promote a greater number of collisions between the reactant molecules, a possible denaturation of the enzyme and a reduction of the stability of the emulsion [7,16,18,19,[22][23][24]. The authors Coteron, A. et al [25], Kristensen, J.B. et al [15] and Paroul, N. et al [16], claim that temperature has three important roles in this type of reaction.…”

Section: Factorial Design and Enzymatic Reactionsmentioning

confidence: 99%

“…Published articles generally study enzymatic reactions through experimental designs based on the final yield of the reaction and invariably conclude that temperature is the most important variable for the studied system [7,10,16,23]. However, this variable trend of influence has a divergent behavior between these studies, even though they used similar temperature ranges.…”

Section: Influence Of Temperature Variable In the Yield Of The Reactionmentioning

confidence: 99%

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Enzyme activation using dynamic manipulation of process variables.

Dantas

Harth

Paris

et al. 2015

JBT

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Experimental design and surface response methodology were used to study the production of radish oil ethyl ester, using Burkholderia cepacia lipase. The estimative of the standard effects were determined as a function of time to analyze the importance of some variables. The results showed the importance of variables, as well the extents of their effect, vary throughout the reaction. Then was possible to analyze the behavior of the reaction medium and to propose situations where higher yields could be obtained. In fact, when the reactor was operated in this way, an 80,1% yield was achieved, much higher than common operation (39.9%). Also, enzymatic activity of ester production was tenfold.

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“…The aim of this work was to investigate the enzymatic acetylation of cis ‐3‐hexen‐1‐ol and 2‐phenylethanol with different acetylating agents, to provide the corresponding esters via esterification and transesterification according to greener chemical approaches, since these compounds are intended for a human consumption. Literature data report the preparation of these acetates with satisfactory conversions but mainly with the use of harmful solvents (eg, n‐hexane, heptane, ACN) and under heating both for cis ‐3‐hexen‐1‐yl acetate and rose aromatic ester 2‐phenylethyl acetate . The use of more eco‐friendly solvents as reaction media or to carry out the synthetic reaction in a solvent‐free systems might contribute to improve the sustainability of a synthetic process.…”

Section: Introductionmentioning

confidence: 99%

Natural flavor ester synthesis catalyzed by lipases

Bayout

Bouzemi

Guo

et al. 2019

Flavour & Fragrance J

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In spite of the fact that several flavors and fragrances are obtained either by chemical synthesis or by extraction from plants, the application of biocatalysis for the sake of a safe and productive pathway by more sustainable chemical processes is the main alternative. The current study focuses on the synthesis of three flavor esters, namely cis‐3‐hexen‐1‐yl acetate, 2‐phenylethyl acetate, and methyl phenylacetate, via transesterification and esterification of the natural corresponding alcohols or acids. The impact of optimizing variables that influence this lipase‐catalyzed synthesis, such as enzyme formulations, solvent‐free media, and acetylating agents, is crucial to achieving higher conversions. The enzymatic transesterification using Novozym 435 afforded cis‐3‐hexen‐1‐yl, and 2‐phenylethyl acetates with high yields (>90%) in green solvents. Similar results were obtained in solvent‐free system, which is more economic for the scaling up of this synthesis. In the case of esterification reactions, the removal of water, formed as a by‐product, with the use of Aquasorb enhanced the conversions as in the case of methyl phenylacetate attained with a conversion of 89% in the presence of Novozym 435. However, this effect was not observed in the larger scale reaction (with 0.85 mol of cis‐3‐hexen‐1‐ol). Instead, the efficient strategy of gradual addition of acetic acid has proven to significantly improve the yield of cis‐3‐hexen‐1‐yl acetate (from 2% up to about 80% in the case of the preparative reaction with 100 mL substrate). Box‐Behnken analysis was also performed to identify the lowest amount of acetylating agent and the shorter time to obtain the highest conversion ratio. This analysis showed that a triacetin/alcohol molar ratio of 1 and 1.75 can be sufficient to obtain a conversion >90% and up to 95%, for cis‐3‐hexen‐1‐yl acetate and 2‐phenylethyl acetate, respectively, similarly to what is obtained with higher triacetin/alcohol molar ratios and comparable reaction time.

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Enzymatic synthesis of rose aromatic ester (2‐phenylethyl acetate) by lipase

Cited by 32 publications

References 30 publications

Metabolic engineering of Escherichia coli for production of 2‐Phenylethylacetate from L‐phenylalanine

Metabolic engineering of Escherichia coli for production of 2‐Phenylethylacetate from L‐phenylalanine

Enzyme activation using dynamic manipulation of process variables.

Natural flavor ester synthesis catalyzed by lipases

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