Production of structured triacylglycerols by acidolysis catalyzed by lipases immobilized in a packed bed reactor

Hita, Estrella; Robles, Alfonso; Camacho, Belén; González, P.; Esteban, Luis; Jiménez, M.J.; Muñío, María M.; Molina, Emilio

doi:10.1016/j.bej.2009.05.015

Cited by 61 publications

(39 citation statements)

References 30 publications

(50 reference statements)

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“…Different Chitopearl beads are produced and they can differ in the type and length of side ligands to be rightly chosen for a particular immobilization. The commercial products utilized in enzyme adsorption also include a group of polyvinyl supports available under the name Lentikats (Kubac et al 2006), as well as the polymer matrices Accurel EP100 (Torres et al 2008) and Accurel MP1000 (Hita et al 2009). …”

Section: Commercial Productsmentioning

confidence: 99%

“…polypropylene (c) Fig. 3 Representative silica surface modifying agents used in enzyme immobilization, a silica particle grafted with glutaraldehyde, b silica particle modified with 3-aminopropyltriethoxysilane, c silica particle functionalized with mercaptopropyltriethoxysilane, d silica particle grafted with vinyltrimethoxysilane membranes Accurel EP100 and Accurel MP1000 (Hita et al 2009), adsorbent Purasorb (Torres et al 2008). Lipases were also immobilized on other materials such as buthyl and octadecyl sepabeads (Branco et al 2010), cotton flannel cloth (Karimpil et al 2012), olive pomace powder (Yucel 2012) and commercial ion exchange resin Lewatit.…”

Section: Immobilized Enzymesmentioning

confidence: 99%

“…These properties can also be adapted by preparing the polymer composites. The synthetic polymers most commonly used as enzyme carriers include: poly(vinyl alcohol) (PVA) (Mendes et al 2012) (commercial product LentiKats) (Kubac et al 2006); crosslinked poly(vinyl alcohol) (Ozturk and Kilinc 2010); poly(N-methylolacrylamide) (Santos et al 2007); polypropylene (commercial products Accurel EP100 (Torres et al 2008) and Accurel MP1000 (Hita et al 2009); polystyrene in the form of foam (Akdogan and Pazarlioglu 2011), in which immobilization is facilitated by a large number of pores; and poly(acrylic acid-co-acrylamide)/ hydrotalcite nanocomposite hydrogels (Zhang et al 2009). An interesting enzyme carrier is the biodegradable and thermo-shrinkable hydroxybutyrate.…”

Section: Organic Carriersmentioning

confidence: 99%

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Enzyme immobilization by adsorption: a review

2014

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Endowed with unparalleled high catalytic activity and selectivity, enzymes offer enormous potential as catalysts in practical applications. These applications, however, are seriously hampered by enzymes' low thermal and chemical stabilities. One way to improve these stabilities is the enzyme immobilization. Among various tested methods of this process that make use of different enzyme-carrier interactions, immobilization by adsorption on solid carriers has appeared most common. According to these findings, in this review we present a comparative analysis of the literature reports on the recent trends in the immobilization of the enzymes by adsorption. This thorough study was prepared in order to provide a deeper understanding of the process. Both carriers, carrier modifiers and procedures developed for effective adsorption of the enzymes are discussed. The review may thus be helpful in choosing the right adsorption scheme for a given enzyme to achieve the improvement of its stability and activity for a specific application.

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Section: Commercial Productsmentioning

confidence: 99%

Section: Immobilized Enzymesmentioning

confidence: 99%

Section: Organic Carriersmentioning

confidence: 99%

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Enzyme immobilization by adsorption: a review

2014

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“…In previous works the results of acidolysis reactions were correlated to an empirical kinetic model [36,37] and to a kinetic model based on the reaction mechanism [38]; in those works was The curve that fits the experimental results in Fig. 1 corresponds to the equation [31,36,39]: and V the reaction mixture volume. Equation (1) was obtained making mass balances to the dispersion reactor and considering that the reaction rate is given by equation:…”

Section: Influence Of Temperature and Solvent Amountmentioning

confidence: 99%

“…The identification of lipidic species by preparative TLC and their quantification by GC was carried out following the methods already described in previous articles [31,32].…”

Section: Analysis Of the Reaction Productsmentioning

confidence: 99%

Production of triacylglycerols rich in palmitic acid at sn-2 position by lipase-catalyzed acidolysis

Jiménez

Esteban

Robles

et al. 2010

Biochemical Engineering Journal

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This paper studies the synthesis of triacylglycerols (TAGs) rich in palmitic acid (PA) at sn-2 position from palm stearin (PS), a vegetable oil highly rich in PA (60%, but only 12.8% of this is located at sn-2 position). These PA rich TAGs were obtained by lipasecatalyzed acidolysis of this oil with free fatty acids (FFAs) highly rich in PA, such as commercial PA (98% PA) and a FFA extract obtained by saponification of PS (60% PA). PA has a melting point of 63 ºC and during the acidolysis reaction the substrates, highly rich in this acid, must remain liquid; therefore high temperatures or solvents must be used. An important objective of this work was to operate without solvent and at the lowest possible temperature. In this acidolysis reaction four factors were firstly studied: type of lipase, temperature, solvent amount and the intensity of treatment (IOT = lipase amount × reaction time/PS amount). The influence of these variables was studied in a stirred tank reactor (STR). The lipases tested were Novozym 435 from Candida antarctica (immobilized on a macroporous acrylic resin), and lipases QLC (immobilized on diatomaceous earth), and QLM (non immobilized), both from Alcaligenes sp., and the one selected was lipase QLC. According to the manufacturer the optimum temperature for this lipase is 65-70 ºC, which allows it to operate without solvent. The best results with lipase QLC (TAGs with 80% PA, both total and at sn-2 position) were obtained with commercial PA, at 65 ºC, a 3:1 FFA/PS molar ratio (1:1 w/w), without solvent and an IOT = 7 g lipase × h/g PS (for example 2.5 g PS, 2.5 g commercial PA, 0.75 g lipase and 24 h). These results were the basis for establishing the operational conditions to obtain PA rich TAGs with the lipase immobilized in a packed bed reactor (PBR), operating by recirculation of the reaction mixture through the lipase bed. In this system TAGs with 75% PA were obtained at an IOT = 8 g lipase × h/g PS. This result and the apparent kinetic constants obtained in both reactors show that the reaction rate is lower in the PBR than in the STR. Subsequently, PA enriched TAGs were separated from FFAs by two procedures: the first one at room temperature and in presence of hexane and the second one at 65 ºC and without hexane. Using the first procedure, 95% of TAGs in the acidolysis reaction mixture were recovered with a purity of 99%. Using the second one, 98% pure TAGs were obtained with a recovery yield of 80%. Therefore, these highly rich PA TAGs can be obtained by acidolysis of PS and PA rich FFAs in solvent-free media, and then these TAGs also can be purified to 98% in absence of hexane, using only a hydroethanolic KOH solution.3

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Application of Yeast Hydrolysate in Extracellular Lipase Production by Geotrichum candidum in Shaken Flasks, Stirred Tank, and Airlift Reactors

et al. 2015

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Lipase production by Geotrichum candidum NRRL Y-552 was studied using an alternative nitrogen source, yeast hydrolysate (Prodex-lac 1 ), and soybean oil as the carbon source and inducer of lipase production. Factorial design and response surface methodologies were applied to obtain optimized conditions for lipase production in shaken flasks, defined as: 3.5 g/100 mL of yeast hydrolysate and 0.7 g/100 mL of soybean oil with an initial pH of 7.0 at 30 8C and 250 rpm. The resulting lipase activity after 48 h was 24.3 U/mL (0.506 U/mL . h), 52 % higher than with peptone under the same conditions (U ¼ the amount of enzyme required to liberate 1 mmol of fatty acid per minute). Lipase production with the optimized medium was conducted in a stirred tank reactor and in an airlift bioreactor, both at 30 8C and 300 rpm; the best results obtained were 15.4 U/mL after 32 h of fermentation (0.481 U/mL.h) and 19.24 U/mL after 32 h of fermentation (0.601 U/mL . h) at 1 vvm, respectively. The results presented here from both bioreactors showed similar results to a previous study with the same microorganism under the same conditions using peptone as a nitrogen source. In addition, yeast hydrolysate is a cheaper nitrogen source than peptone and yeast extract, which permits a cost reduction above 90 % under similar conditions.

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Production of structured triacylglycerols by acidolysis catalyzed by lipases immobilized in a packed bed reactor

Cited by 61 publications

References 30 publications

Enzyme immobilization by adsorption: a review

Enzyme immobilization by adsorption: a review

Production of triacylglycerols rich in palmitic acid at sn-2 position by lipase-catalyzed acidolysis

Application of Yeast Hydrolysate in Extracellular Lipase Production by Geotrichum candidum in Shaken Flasks, Stirred Tank, and Airlift Reactors

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