Lipase‐catalyzed synthesis of chiral triglycerides

Chandler, Ian C.; Quinlan, Paul T.; McNeill, Gerald P.

doi:10.1007/s11746-998-0087-7

Cited by 17 publications

(13 citation statements)

References 15 publications

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“…This assumption has been done to simplify the development and application of the proposed model, however there is experimental evidence that the 1 and 3 positions are significantly different at low conversions for the Rhizomucor miehei lipase. [17][18][19] However, this circumstance has no influence on the obtained results because the 1(3), 2-diglycerides are considered as an unique component.…”

Section: Modelling: Equilibrium and Kinetic Equations 31 Equilibriummentioning

confidence: 99%

Kinetics of lipase‐catalysed interesterification of triolein and caprylic acid to produce structured lipids

Páez

Medina

Rubio

et al. 2003

J of Chemical Tech & Biotech

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The influence of the molar ratio caprylic acid/triolein, enzyme concentration and water content on the kinetics of the interesterification reaction of triolein (TO) and caprylic acid (CA) were studied. The enzyme used was the 1,3-specific Rhizomucor miehei lipase. Data modelling was based on a simple scheme in which the acid was only incorporated in positions 1 and 3 of the glyceride backbone. In addition, it was assumed that positions 1 and 3 of the triglycerides were equivalent and that the events at position 1 did not depend on the nature of the fatty acid in position 3 and vice versa. Monoglycerides and diglycerides were not detected during the experiments. This was attributed to the low water content of the immobilised enzyme particles. The value of the equilibrium constant, K, for the exchange of caprylic and oleic acids was 2.7, which indicated that the incorporation of caprylic acid into triglycerides was favoured compared with the incorporation of oleic acid. Simple first order kinetics could describe the interesterification reaction. Using this model and the calculated equilibrium constant, the apparent kinetic constants were calculated. The model fitted all the experimental data except for the CA/TO molar ratios larger than 6. Moreover, the interesterification reaction rate had a maximum value at CA/TO molar ratios of 4-6 mol mol À1.

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Section: Modelling: Equilibrium and Kinetic Equations 31 Equilibriummentioning

confidence: 99%

Kinetics of lipase‐catalysed interesterification of triolein and caprylic acid to produce structured lipids

Páez

Medina

Rubio

et al. 2003

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

show abstract

“…The high stereospecificity of some lipases makes the synthesis of such triacylglycerols possible [49]. It was found that Rhizomucor miehei lipase shows stereospecificity towards sn-1 position [26] and some other lipases had specificity towards sn-3 position [74]. Therefore, chiral triacylglycerols can be produced if only mono-incorporated products are proceeded.…”

Section: Developed and Marketed Productsmentioning

confidence: 99%

Production of specific-structured triacylglycerols by lipase-catalyzed reactions: a review

2000

Eur. J. Lipid Sci. Technol.

320

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Regiospecificity is one of the major advantages of using lipase technology for the modification of oils and fats to produce high‐value added products, such as cocoa butter equivalents, human milk fat substitutes, and other specific‐structured lipids. Due to the high cost of biocatalysts, the mainstream applications of lipases for normal oils and fats are still limited. Therefore, positional specificity of lipases has the priority and will be the target property to be exploited for commercial and industrial developments, because no chemical method has such a specificity and is promising or possible for this task. In this paper, encouraging products resulting from this regiospecificity are reviewed together with the critical evaluation of their reaction schemes, side reactions and by‐products, sources of substrate oils and acyl donors, and production processes.

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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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Lipase‐catalyzed synthesis of chiral triglycerides

Cited by 17 publications

References 15 publications

Kinetics of lipase‐catalysed interesterification of triolein and caprylic acid to produce structured lipids

Kinetics of lipase‐catalysed interesterification of triolein and caprylic acid to produce structured lipids

Production of specific-structured triacylglycerols by lipase-catalyzed reactions: a review

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

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