A New Immobilized Positional Nonspecific Lipase for Fat Modification and Ester Synthesis

Heldt-Hansen, Hans Peter; Ishii, M.; Patkar, Shamkant; Hansen, Thorkild B.; Eigtved, P.

doi:10.1021/bk-1989-0389.ch011

Cited by 34 publications

(22 citation statements)

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“…Previous reports on acyl group selectivity of immobilized C. antarctica B lipase have revealed that this enzyme is not very selective within the group of n ‐acyl donors of chain lengths C6−C18 in acidolysis reactions with trioctanoylglycerol (Heldt‐Hansen et al, 1989) and in esterification reactions with n ‐octanol in hexane (Kirk et al, 1992). This property was also noted for esterification reactions with C4−C16 FA and either n ‐propanol or 2‐propanol in hexane (Arsan, 1997).…”

Section: Resultsmentioning

confidence: 99%

“…In this work, we sought to determine “intrinsic” chain length selectivity toward fatty acid (FA) substrates for Pseudomonas cepacia , Rhizomucor miehei , and Candida antarctica B lipases in esterification reactions. These lipases are recognized as being efficient biocatalysts in microaqueous media (Heldt‐Hansen et al, 1989; Gilbert, 1993; Martinelle and Hult, 1995; Hariyadi and Parkin, 1997; Ader et al, 1997) and exhibit different degrees of regioselectivity from nearly strictly sn ‐1,3‐regioselective ( R. miehei ) to nonregioselective ( C. antarctica ) (Heldt‐Hansen et al, 1989; Ota et al 1996; Ader et al, 1997). Thus, the selected lipases are generally representative of the spectrum of options available for almost any lipase‐mediated lipid transformation.…”

Section: Introductionmentioning

confidence: 99%

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Comparative Fatty Acid Selectivity of Lipases in Esterification Reactions with Glycerol and Diol Analogues in Organic Media

Lee

Parkin

2000

Biotechnol. Prog.

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Reaction selectivity of Pseudomonas cepacia, Rhizomucor miehei, and Candida antarctica B lipases was assessed in multicompetitive esterification reaction mixtures containing an homologous series of n-chain even carbon number fatty acid (FA; C4-C18) substrates and a single alcohol cosubstrate (glycerol, 1,2-propanediol (1,2-PD), or 1, 3-propanediol (1,3-PD)) in tert-butyl methyl ether at water activity of 0.69 or 0.90 and a reaction temperature of 35 degrees C. For P. cepacia lipase, the ordinal patterns of FA selectivities observed were, with glycerol, C8 > C10, C6, C16 > other FA; with 1,2-PD and 1, 3-PD, C16 > C8 > C14 > other FA. For R. miehei lipase, the ordinal patterns of FA selectivities observed were, with glycerol, C8 > C12 > C10, C14 > other FA; with 1,2-PD and 1,3-PD, C8 > C12 > other FA. For C. antarctica B lipase, the ordinal patterns of FA selectivities observed were, with glycerol, C8 > C10, C6, C12 > other FA; with 1, 2-PD, C8 > C10, C6 > other FA; and with 1,3-PD, C8 > C10 > C6 > other FA. The differences in selectivity among FA ranged up to 16-fold, depending upon the lipase and alcohol cosubstrate used. These findings represent intrinsic and substrate-modulated features of FA selectivities that are of particular relevance to the use of lipases for acylglycerol synthesis reactions.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Comparative Fatty Acid Selectivity of Lipases in Esterification Reactions with Glycerol and Diol Analogues in Organic Media

Lee

Parkin

2000

Biotechnol. Prog.

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“…Candida antartica lipase B is probably also a good catalyst for this reaction. However, reports in the literature show that this enzyme, at least under some conditions, is not completely selective for the sn-1 position [24]. A water activity of 0.22 was used to make it possible to achieve equilibration of fatty acids.…”

Section: Synthesis Of Regioisomers Of Pc Containing Epa or Dhamentioning

confidence: 99%

Enzymatic and chemical synthesis of phosphatidylcholine regioisomers containing eicosapentaenoic acid or docosahexaenoic acid

Lyberg

Adlercreutz

2005

Euro J Lipid Sci & Tech

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Regioselective incorporation of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) into phosphatidylcholine (PC) was carried out using enzymatic and chemical synthesis. Incorporation at the sn-1 position was successfully achieved by lipasecatalysed esterification of 2-palmitoyl-lysophosphatidylcholine (LPC), although in most cases, the enzymes incorporated EPA and DHA at lower rates than other fatty acids. For the incorporation of DHA, Candida antarctica lipase B was the only useful enzyme, while incorporation of EPA was efficiently carried out using either this enzyme or Rhizopus arrhizus lipase. The highest yields in the lipase-catalysed reactions were obtained at the lowest water activity (close to 0). However, by carrying out the reactions at a higher water activity of 0.22, more EPA and DHA were incorporated. Esterification of 2-palmitoyl-LPC with pure EPA at this water activity converted 66 mol-% of LPC to PC using Rhizopus arrhizus lipase as catalyst. When the fatty acid was DHA and the catalyst Candida antarctica lipase B, 45 mol-% of PC was obtained. For incorporation of EPA and DHA at the sn-2 position, phospholipase A 2 was used, but the reaction was very slow. Chemical coupling of 1-palmitoyl-LPC and EPA or DHA was more efficient, resulting in complete conversion of LPC.

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“…The fourth of the lipases (CALA) is reported to show a sn-2-regioselectivity [32,33], although such preference in the structure of triacylglycerols (TAG) is not sufficient to selective synthesis of 1,3-diglycerides or 2-monoglycerides [34]. Therefore, for practical interesterifications, CALA has been reported rather as a nonselective lipase [35]. All enzymes were used in immobilized form, which made it possible to carry out the reactions in the presence of solvent and at higher temperatures.…”

Section: Screening Of Enzymesmentioning

confidence: 99%

Production of Structured Phosphatidylcholine with High Content of Myristic Acid by Lipase-Catalyzed Acidolysis and Interesterification

Chojnacka

Gładkowski

2018

Catalysts

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Synthesis of structured phosphatidylcholine (PC) enriched with myristic acid (MA) was conducted by acidolysis and interesterification reactions using immobilized lipases as catalysts and two acyl donors: trimyristin (TMA) isolated from ground nutmeg, and myristic acid obtained by saponification of TMA. Screening experiments indicated that the most effective biocatalyst for interesterification was Rhizomucor miehei lipase (RML), whereas for acidolysis, the most active were Thermomyces lanuginosus lipase (TLL) and RML. The effect of the molar ratio of substrates (egg-yolk PC/acyl donor), enzyme loading, and different solvent on the incorporation of MA into PC and on PC recovery was studied. The maximal incorporation of MA (44 wt%) was achieved after 48 h of RML-catalyzed interesterification in hexane using substrates molar ratio (PC/trimyristin) 1/5 and 30% enzyme load. Comparable results were obtained in toluene with 1/3 substrates molar ratio. Interesterification of PC with trimyristin resulted in significantly higher MA incorporation than acidolysis with myristic acid, particularly in the reactions catalyzed by RML.

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A New Immobilized Positional Nonspecific Lipase for Fat Modification and Ester Synthesis

Cited by 34 publications

References 0 publications

Comparative Fatty Acid Selectivity of Lipases in Esterification Reactions with Glycerol and Diol Analogues in Organic Media

Comparative Fatty Acid Selectivity of Lipases in Esterification Reactions with Glycerol and Diol Analogues in Organic Media

Enzymatic and chemical synthesis of phosphatidylcholine regioisomers containing eicosapentaenoic acid or docosahexaenoic acid

Production of Structured Phosphatidylcholine with High Content of Myristic Acid by Lipase-Catalyzed Acidolysis and Interesterification

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