Interfacial catalysis by lipases

Miled, Nabil; Beisson, Frédéric; De, Josiane; De, Alain; Arondel, Vincent; Verger, Robert

doi:10.1016/s1381-1177(00)00041-2

Cited by 61 publications

(29 citation statements)

References 11 publications

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“…X-ray crystallographic studies revealed that TLL is a typical lid-containing lipase. In its open form the lid is displaced and the active center is exposed to the medium, which often results in an increase in enzyme activity (interfacial activation) [42]. The active center of lipase is very sensitive to any changes in surrounding such as the experimental conditions, thus, the immobilization strategy employed etc.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

et al. 2015

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Section: Introductionmentioning

confidence: 99%

Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

et al. 2015

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“…The hydrophobic supports resemble the surface of the enzyme's natural substrate and hence the enzyme binds to them with high affinity. When the procedure is carried out under conditions of low ionic strength, other water soluble proteins are excluded and the process becomes highly selective for the lipases (4). Hydrophobic areas surrounding the active site and located in the internal face of the lid are involved in this adsorption process.…”

Section: Introductionmentioning

confidence: 99%

Bacillus sp. PS35 Lipase-Immobilization on Styrene-Divinyl Benzene Resin and Application in Fatty Acid Methyl Ester Synthesis

Palanisamy¹,

Kumaresan²,

Jeyaseelan³

2015

Iran J Biotech

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Background:Lipase is an enzyme with immense application potential. Ester synthesis by lipase catalysis in organic media is an area of key industrial relevance. Enzymatic preparations with traits that cater to the needs of this function are hence being intensely researched. Objective: The objectives of the study were to immobilize the lipase from Bacillus sp. PS35 by cross-linking and adsorption onto styrene-divinyl benzene (Sty-Dvb) hydrophobic resin and to comparatively characterize the free and immobilized lipase preparations. The work also aimed to apply the immobilized lipase for catalysing the fatty acid methyl ester (FAME) synthesis from palm oil and optimize the process parameters for maximizing the yield. Materials and Methods: In this study, the purified lipase from Bacillus sp. PS35 was immobilized by adsorption onto styrene-divinyl benzene hydrophobic resin with gluteraldehyde cross-linking. Results: The immobilized enzyme showed better pH and temperature stabilities than the free lipase. Organic solvent stability was also enhanced, with the relative activity in the presence of methanol being shifted from 53% to 81%, thereby facilitating the enzyme's application in fatty acid methyl ester synthesis. It exhibited remarkable storage stability over a 30-day period and after 20 repetitive uses. Cross-linking also reduced enzyme leakage by 49%. The immobilized lipase was then applied for biodiesel production from palm oil. Methanol and oil molar ratio of 5:1, three step methanol additions, and an incubation temperature of 50°C were established to be the ideal conditions favoring the transesterification reaction, resulting in 97% methyl ester yield. Conclusions: These promising results offer scope for further investigation and process scale up, permitting the enzyme's commercial application in a practically feasible and economically agreeable manner.

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“…are considered as hydrolases that catalyse the hydrolysis of waterinsoluble esters at water/oil interfaces. Most of them exhibit an interfacial catalytic kinetics [6]. In addition, lipases are also able to catalyse different reactions, namely esterification of free fatty acids (FFA), alcoholysis of a donor ester (transesterification), and combined reactions resulting in the exchange of acyl groups between two esters (interesterification) or between an ester and an FFA (acidolysis).…”

Section: Introductionmentioning

confidence: 99%

Lipase/acyltransferase‐catalysed interesterification of fat blends containing n‐3 polyunsaturated fatty acids

Osório

Dubreucq

Fonseca

et al. 2009

Euro J Lipid Sci & Tech

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The lipase/acyltransferase from Candida parapsilosis is an original biocatalyst that preferentially catalyses alcoholysis over hydrolysis in biphasic aqueous/organic media. In this study, the performance of the immobilised biocatalyst in the interesterification in solvent-free media of fat blends rich in n-3 polyunsaturated fatty acids (n-3 PUFA) was investigated. The interesterification activity of this biocatalyst at a water activity (a w ) of 0.97 was similar to that of commercial immobilised lipases at a w values lower than 0.5. Thus, the biocatalyst was further used at an a w of 0.97. Response surface modelling of interesterification was carried out as a function of medium formulation, reaction temperature (55-75 7C) and time (30-120 min). Reaction media were blends of palm stearin (PS), palm kernel oil and triacylglycerols (TAG) rich in n-3 PUFA ("EPAX 4510TG"; EPAX AS, Norway). The best results in terms of decrease in solid fat content were observed for longer reaction time (.80 min), lower temperature (55-65 7C), higher "EPAX 4510TG" content and lower PS concentration. Reactions at higher temperature led to final interesterified fat blends with lower free fatty acid contents. TAG with high equivalent carbon number (ECN) were consumed while acylglycerols of lower ECN were produced.

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Interfacial catalysis by lipases

Cited by 61 publications

References 11 publications

Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking

Bacillus sp. PS35 Lipase-Immobilization on Styrene-Divinyl Benzene Resin and Application in Fatty Acid Methyl Ester Synthesis

Lipase/acyltransferase‐catalysed interesterification of fat blends containing n‐3 polyunsaturated fatty acids

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