Studies on synthesis of short chain alkyl esters catalyzed by goat pregastric lipase

Lai, Douglas T.; O’Connor, Charmian J.

doi:10.1016/s1381-1177(99)00007-7

Cited by 29 publications

(15 citation statements)

References 26 publications

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“…This is probably due to progressively higher steric hindrance by the methyl groups in the proximity of the hydroxyl group. Results consistent with our work have been observed in previous studies focusing on the effects of the structures of alcohols on ester synthesis catalyzed by lipases [39][40][41]. In general, Fe 3 O 4 -collagen immoblilzed lipases displayed high activity and specificity for butyrate synthesis in an n-hexane medium.…”

Section: Synthesis Of Butyrate By Mnp-col-ilsupporting

confidence: 92%

“…Interestingly, Table 3 also showed that different alcohol isomers exhibited different yields, with the following order: n-alcohol > iso-alcohol > tert-alcohol. This could be explained by the influence of steric effects [36,39]. The conversion of iso-butanol (61.9%) and tert-butanol (6.2%) was significantly lower compared with n-butanol (82.7%).…”

Section: Synthesis Of Butyrate By Mnp-col-ilmentioning

confidence: 98%

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Immobilization of Lipases on Magnetic Collagen Fibers and Its Applications for Short-Chain Ester Synthesis

Song

Chen

et al. 2017

Catalysts

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Magnetic nanoparticles (MNp) Fe 3 O 4 were prepared by chemical coprecipitation, and introduced onto collagen fibers to form magnetic collagen support (MNp-Col) for enzyme immobilization. Candida rugosa lipase has been successfully immobilized on MNp-Col supports by a covalent bond cross-linking agent, glutaraldehyde. The characteristics of MNp-Col and the immobilized lipase were investigated. The immobilized lipase displayed sound magnetic separation abilities in both aqueous and organic media. The activity of the immobilized lipase reached 2390 U/g under optimal conditions. The MNp-Col immobilized lipase shows broadened temperature and pH ranges for hydrolysis of olive oil emulsion. For synthesis of butyrate esters in an n-hexane medium, the yield changes through use of different alcohols, among which, butyric butyrate showed the highest yield. The prepared magnetic collagen fiber provides separation support for enzyme immobilization and has the potential to be used in other biotechnology fields.

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Section: Synthesis Of Butyrate By Mnp-col-ilsupporting

confidence: 92%

Section: Synthesis Of Butyrate By Mnp-col-ilmentioning

confidence: 98%

Immobilization of Lipases on Magnetic Collagen Fibers and Its Applications for Short-Chain Ester Synthesis

Song

Chen

et al. 2017

Catalysts

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“…The low esterification rates and yields for ethyl esters can also be attributed to an inhibition effect of the ethanol on enzyme activity (de Barros et al, 2009a;Lai and O'Connor, 1999) but also to the high solubility of ethanol in the continuous phase (water) and, consequently, low concentration inside the hydrophobic droplets.…”

Section: The Effect Of Stepwise Addition Of Alcohol On the Amano Lipamentioning

confidence: 99%

Miniemulsion as efficient system for enzymatic synthesis of acid alkyl esters

Barros

Fonseca

Aschenbrenner

et al. 2010

Biotech & Bioengineering

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The aim of this work is to devise an efficient enzymatic process for the production of linear alkyl esters in aqueous miniemulsion systems. The esterification reactions of linear alcohols and carboxylic acids were performed with three different enzymes, commercial Amano lipase PS from Pseudomonas cepacia, Lipase type VII from Candida rugosa, and lyophilized Fusarium solani pisi cutinase expressed in Saccharomyces cerevisiae SU50. The miniemulsion system shows a high potential for the synthesis of linear alkyl esters, for example, hexyl octanoate, which could be synthesized with an ester yield of 94% using Amano lipase PS. Even with hydrophilic alcohols as ethanol, ethyl decanoate could be obtained with a concentration of 0.45 M and a yield of 62% using F. s. pisi cutinase as catalyst. High esterification rates for ethyl- and hexyloleate in miniemulsion showed a significant shift in cutinase selectivity towards longer chain length carboxylic acids. The stepwise addition of the alcohol led to an increase of the esterification yield. Moreover, increasing the amount of dispersed organic phase, mainly consisting of the substrates, led to a significant increase of the final ester concentration (e.g., concentration of 1.4 M for ethyl decanoate for the esterification with Amano Lipase PS).

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“…In addition, lipases can also catalyse the hydrolysis and synthesis of a broad range of natural and unnatural esters, while retaining high enantio or regioselectivity (Pandey et al 1999). This combination of broad substrate range and high selectivity makes lipases ideal catalysts for organic synthesis (Lai & O'Connor 1999;Villeneuve et al 2000).…”

Section: Introductionmentioning

confidence: 99%

“…Ester synthesis by lipases can be performed at room temperature and pressure, providing an energy-saving procedure under neutral pH in reaction vessels operated either batchwise or continuously (Lai & O'Connor 1999). Therefore, the products obtained are qualitatively purer than those obtained by chemical catalysis, which tends to be unspecific, and consequently generates several byproducts (Roy & Bhattacharyya 1993).…”

Section: Introductionmentioning

confidence: 99%

Optimization of Lipase-catalysed Synthesis of Butyl Butyrate Using a Factorial Design

Santos¹,

Castro²

2006

World J Microbiol Biotechnol

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A lipase from Candida rugosa immobilized on styrene-divinylbenzene copolymer was used to catalyse the direct esterification of butanol and butyric acid. A factorial design was employed to evaluate the effects of temperature (37-50°C), substrate molar ratio of butyric acid to butanol (0.6 to 2.0) and enzyme amount (0.2-0.4 g) on the ester yield. The main effects were fitted by multiple regression analysis to a linear model and maximum ester yield could be obtained working at 41°C with 0.4 g of lipase. The mathematical model obtained, representing the ester yield has been found to describe adequately the experimental results. Under optimal conditions, concentration of 32.4 g butyl butyrate/l that corresponds to a yield of 75% was obtained.

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Studies on synthesis of short chain alkyl esters catalyzed by goat pregastric lipase

Cited by 29 publications

References 26 publications

Immobilization of Lipases on Magnetic Collagen Fibers and Its Applications for Short-Chain Ester Synthesis

Immobilization of Lipases on Magnetic Collagen Fibers and Its Applications for Short-Chain Ester Synthesis

Miniemulsion as efficient system for enzymatic synthesis of acid alkyl esters

Optimization of Lipase-catalysed Synthesis of Butyl Butyrate Using a Factorial Design

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