Immobilized lipase-catalysed synthesis of cinnamyl laurate in non-aqueous media

Yadav, Ganapati D.; Dhoot, Shrikant B.

doi:10.1016/j.molcatb.2008.06.013

Cited by 63 publications

(30 citation statements)

References 21 publications

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“…Enzymatic catalysis has the advantage of higher reaction activity, mild reaction conditions, simple post-treatment and is contamination-free, giving it great potential to solve the problems that exist in the conventional approach. Although several publications have appeared on the enzyme-catalyzed esterification of lactic acid and other fatty acids with alcohol (Roenne et al 2005;Abdullah et al 2009;Mahapatra et al 2009;Yadav & Dhoot 2009), and on glucose ester synthesis , there is a dearth of information on the enzyme-catalyzed synthesis of ethyl lactate (Zhao et al 2006). In Roenne's work, the esterification of lactic acid with C 6 -C 18 alcohols was systematically investigated (Roenne et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Optimization and kinetic study of immobilized lipase-catalyzed synthesis of ethyl lactate

Sun

Jiang

Zhou

et al. 2010

Biocatalysis and Biotransformation

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Enzymatic synthesis of ethyl lactate catalyzed by immobilized lipase has been investigated. The reaction variables (including the molar ratio of ethanol to acid, total substrate amount, temperature, reaction time and rotation speed) were selected in accordance with the Plackett-Burman design and were further optimized via response surface methodology. The molar ratio of ethanol to acid, total substrate amount and reaction time were screened out as significant variables for the optimization study. A 20-run, full-factorial, central composite design was used to construct the statistical model and the optimal conditions obtained were as follows: molar ratio of ethanol to acid of 8.3:1, total substrate amount of 0.4 g, reaction time of 26.87 h with temperature of 55°C and rotation speed of 150 rpm. Under the optimal conditions, the yield of ethyl lactate was up to 24.32%; close to the 25.13% obtained using the commercial lipase, Novozym 435. Due to the low cost and simple immobilization process, the lipase prepared in the present work could have great potential in enzymatic applications. Additionally, a kinetic model with inhibition by both ethanol and lactic acid following a ping-pong bi-bi mechanism was proposed.

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Section: Introductionmentioning

confidence: 99%

Optimization and kinetic study of immobilized lipase-catalyzed synthesis of ethyl lactate

Sun

Jiang

Zhou

et al. 2010

Biocatalysis and Biotransformation

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“…Higher yield of enantioselective product is obtained in final 37 step when pure monoacetylated product is used as substrate. 38 Lipases are the most important group of biocatalysts in non-39 aqueous enzymology; they do not need cofactors for assisting the 40 reaction, are capable of differentiating the chiral centers and have 41 extensive substrate specificity [23][24][25][26][27][28][29][30][31][32]. Lipases are widely 42 present in different sources which include bacteria and fungi 43 and hence can be readily available for biotransformation of 44 interest.…”

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confidence: 99%

Kinetics and mechanism of regioselective monoacetylation of 3-aryloxy-1,2-propandiols using immobilized Candida antarctica lipase

Pawar

Yadav

2015

Journal of Industrial and Engineering Chemistry

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“…2 shows results of conversion of cetyl octanoate for the three immobilized lipase at the different pressure. Of the three lipases In other studies, Novozym 435 has also been shown to be very active and useful in catalyzing the synthesis of esters [21][22][23][24]. For this reason, Novozym Ò 435 was employed for the following experiments in this study.…”

Section: Efficacy Of Different Catalystsmentioning

confidence: 99%

Optimization of Lipase‐Catalyzed Synthesis of Cetyl Octanoate in Supercritical Carbon Dioxide

Kuo

Chu

et al. 2011

J Americ Oil Chem Soc

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Cetyl octanoate, a wax ester of 24 carbons, is widely used in the cosmetic industry as a base oil. The current work focuses on lipase-catalyzed synthesis of cetyl octanoate in supercritical carbon dioxide (SC-CO2) by esterification of cetyl alcohol and octanoic acid. Three immobilized lipases were screened, and 15 reaction conditions were tested in order to find the combination for maximal yield. The results showed that Novozym 435 was the best catalyst for the synthesis, and a reaction time of 20 min was adequate for a maximal yield. Response surface methodology (RSM) with a 3-factor- 3-level Box-Behnken design was employed to evaluate the effects of synthesis parameters, including reaction temperature (35–75 C), pressure (8.27–12.41 MPa), and enzyme amount (5–15% wt of cetyl alcohol). A model for the synthesis was developed and the optimum conditions could be predicted to be reaction pressure of 10.22 MPa, reaction temperature of 63.70 C, and enzyme amount of 11.20%. An experiment was performed under this optimum condition and a yield of 99.5% was obtained. This experimental yield correlated well with the predicted value of yield (97.6%). We concluded that, in a SC-CO2 system, nearly 100% molar conversion of cetyl octanoate could be obtained by immobilized Novozym 435 in a short reaction time (20 min) under the predicted optimal conditions

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Immobilized lipase-catalysed synthesis of cinnamyl laurate in non-aqueous media

Cited by 63 publications

References 21 publications

Optimization and kinetic study of immobilized lipase-catalyzed synthesis of ethyl lactate

Optimization and kinetic study of immobilized lipase-catalyzed synthesis of ethyl lactate

Kinetics and mechanism of regioselective monoacetylation of 3-aryloxy-1,2-propandiols using immobilized Candida antarctica lipase

Optimization of Lipase‐Catalyzed Synthesis of Cetyl Octanoate in Supercritical Carbon Dioxide

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