Two‐step enzymatic reaction for the synthesis of pure structured triacylglycerides

Soumanou, Mohamed M.; Bornscheuer, Uwe T.; Schmid, Rolf D.

doi:10.1007/s11746-998-0209-2

Cited by 86 publications

(69 citation statements)

References 26 publications

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“…They are synthesized either to provide specific metabolic effects for nutritive or therapeutic purposes, or to improve physical and/or chemical characteristics of lipids [4][5]. ST containing LCFA at the sn2-position and medium-chain fatty acids at the sn1-and sn3-positions (MLM) were synthesized from various oils using immobilized lipases as catalysts in organic solvents or solventfree conditions by one-step transesterification or a twostep reaction [6][7][8]. Those ST-bearing PUFA are of major current interest.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of 2‐monoglycerides by alcoholysis of palm oil and tuna oil using immobilized lipases

Wongsakul

Prasertsan

Bornscheuer

et al. 2003

Euro J Lipid Sci & Tech

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Synthesis of 2-monoglycerides by alcoholysis of palm oil and tuna oil using immobilized lipasesCommercial immobilized lipases were used for the synthesis of 2-monoglycerides (2-MG) by alcoholysis of palm and tuna oils with ethanol in organic solvents. Several parameters were studied, i.e., the type of immobilized lipases, water activity, type of solvents and temperatures. The optimum conditions for alcoholysis of tuna oil were at a water activity of 0.43 and a temperature of 60 °C in methyl-tert-butyl ether for ~12 h. Although immobilized lipase preparations from Pseudomonas sp. and Candida antarctica fraction B are not 1,3-regiospecific enzymes, they were considered to be more suitable for the production of 2-MG by the alcoholysis of tuna oil than the 1,3-regiospecific lipases (Lipozyme RM IM from Rhizomucor miehei and lipase D from Rhizopus delemar). With Pseudomonas sp. lipase a yield of up to 81% 2-MG containing 80% PUFA (poly-unsaturated fatty acids) from tuna oil was achieved. The optimum conditions for alcoholysis of palm oil were similar as these of tuna oil alcoholysis. However, lipase D immobilized on Accurel EP100 was used as catalyst at 40 °C with shorter reaction times (12 h). This lead to a yield of ~ 60% 2-MG containing 55.0-55.7% oleic acid and 18.7-21.0% linoleic acid.

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Section: Introductionmentioning

confidence: 99%

Synthesis of 2‐monoglycerides by alcoholysis of palm oil and tuna oil using immobilized lipases

Wongsakul

Prasertsan

Bornscheuer

et al. 2003

Euro J Lipid Sci & Tech

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“…Thus, the importance of the water content of the system was shown (Green and Nakajima, 1998;Haraldsson and Thorarensen, 1999;McNeill and Sonnet, 1995;Rosu et al, 1999;Villeneuve et al, 1998). Some studies reported that the water thermodynamic activity (a w ) is conditioning the lipase spatial structure and thus its enzymatic activity either toward synthesis or hydrolysis (Chandler et al, 1998;Soumanou et al, 1998b;Svensson et al, 1994;Valivety et al, 1992Valivety et al, , 1994Villeneuve et al, 1997a;Lee and Foglia, 2000). For synthesis reactions performed with water-free substrates and in a solventfree system, the aqueous phase is limited to the one coming from the enzyme preparation.…”

Section: Introductionmentioning

confidence: 99%

Plant lipases: Biocatalyst aqueous environment in relation to optimal catalytic activity in lipase‐catalyzed synthesis reactions

Caro

Pina

Turon

et al. 2002

Biotech & Bioengineering

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Adsorption and desorption isotherms of two commercial enzyme preparations of papain and bromelain were determined with a Dynamic Vapor System. The Guggenheim-Anderson-deBoer (GAB) modeling of the obtained sorption isotherms allowed the definition of different levels of hydration of those samples. Afterward, these enzyme preparations were used as biocatalysts in water and solvent-free esterification and alcoholysis reactions. The evolution of the obtained fatty acid ester level as a function of the initial hydration level of the biocatalyst, i.e., thermodynamic water activity (a(w)) and water content, was studied. The results show an important correlation between the initial hydration level of the biocatalyst and its catalytic activity during the lipase-catalyzed synthesis reactions. Thus, the Carica papaya lipase (crude papain preparation) catalytic activity is highly dependent on the biocatalyst hydration state. The optimized synthesis reaction yield is obtained when the a(w) value of the enzyme preparation is stabilized at 0.22, which corresponds to 2% water content. This optimal level of hydration occurs on the linear part of the biocatalyst's sorption isotherm, where the water molecules can form a mono- or multiple layer with the protein network. The synthesis reaction yield decreases when the a(w) of the preparation is higher than 0.22, because the excess water molecules modify the system equilibrium leading to the reverse and competitive reaction, i.e., hydrolysis. These results show also that an optimal storage condition for the highly hydrophilic crude papain preparation is a relative humidity strictly lower than 70% to avoid an irreversible structural transition leading to a useless biocatalyst. Concerning the bromelain preparation, no effect of the hydration level on the catalytic activity during esterification reactions was observed. This biocatalyst has too weak a catalytic activity which makes it difficult to observe any differences. Furthermore, the bromelain preparation is far more hydrophobic as it adsorbs only 18 g of water per 100 g of dry material at a(w) around 0.90. No deliquescence of this enzymatic preparation is observed at this a(w) value.

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“…In the literature, because of its nutritional importance, ST has received many attentions [7][8][9][10][11]. Reactions were performed for the production of pure ST using one or two-step enzymatic process.…”

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confidence: 99%

Activity and stability of immobilized lipases in lipase-catalyzed modification of peanut oil

Soumanou

Edorh²,

Bornscheuer

2004

OCL

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Key words: interesterification reaction, peanut oil, microbial lipases, immobilization, structured triacylglycerols, stabilityLipid modification strategies for industry include processes such as fractionation, hydrogenation and interesterification. While each of the two first processes has specific uses and advantages, interesterification reaction offers the greatest potential application [1]. It includes three approaches: acidolysis, alcoholysis and transesterification. Chemically, it can be induced by the use of alkali catalysts in a reaction which lacks specificity and offers little or no control over the positional distribution of fatty acids in the final product [1,2].To overcome such difficulties, enzymatic approach is used. Applied biocatalysts are microbial lipases and are based mainly on their specificity. They are divided in two main groups: random lipases, which cleave fatty acids at all position on the glycerol molecule (e.g. lipases from Candida antarctica, Candida rugosa, Corynebacterium acnes and Staphylococcus aureus) and sn-1, 3-specific lipases, which act preferentially at the sn-1 and sn-3 positions of the glycerol molecule (e.g. lipases from Rhizomucor miehei, Rhizopus oryzae, Aspergillus niger, etc.) [3]. The second group of lipases show specificity for particular fatty acids. An example is the lipase from Geotrichum candidum, which has a marked specificity for long-chain fatty acids that contain cis-9 unsaturation [4].The microbial lipases described above have been used successfully as biocatalysts in modification of oils and fats via hydrolysis, esterification and interesterification [5,6].The lipase-catalyzed interesterification process in food industry can be used for the production of triacylglycerols with specific physical properties and it also opens possibilities for making so-called structured triacylglycerols (ST). In the literature, because of its nutritional importance, ST has received many attentions [7][8][9][10][11]. Reactions were performed for the production of pure ST using one or two-step enzymatic process. In terms of reaction conditions, crucial role of support for immobilization and water activity on the synthesis of ST were also reported [12][13][14][15]. Between the two enzymatic processes used for the production of ST, one step reaction, namely interesterification of a mixture of triglycerides received many attentions, because of its application for industrial purposes. The one step interesterification reaction appears very easy to carry out, but many reactions involved among various triglycerides molecules make difficult analytical analysis of products. However, species fractions of the products under substrate molar ratio have been theoretically proposed and the kinetic model of the transesterification of a mixture of mediumchain fatty acid triglycerides (MCT) and long-chain fatty acid triglycerides (LCT) was developed [16][17][18]. Based on this kinetic model, the rate constant of interesterification reaction was determined [18]. On the other hand, some minor comp...

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Two‐step enzymatic reaction for the synthesis of pure structured triacylglycerides

Cited by 86 publications

References 26 publications

Synthesis of 2‐monoglycerides by alcoholysis of palm oil and tuna oil using immobilized lipases

Synthesis of 2‐monoglycerides by alcoholysis of palm oil and tuna oil using immobilized lipases

Plant lipases: Biocatalyst aqueous environment in relation to optimal catalytic activity in lipase‐catalyzed synthesis reactions

Activity and stability of immobilized lipases in lipase-catalyzed modification of peanut oil

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