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

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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Study of Soybean Oil Hydrolysis Catalyzed by Thermomyces lanuginosus Lipase and Its Application to Biodiesel Production via Hydroesterification

Enzyme Research ◽

10.4061/2011/618692 ◽

2011 ◽

Vol 2011 ◽

pp. 1-8 ◽

Cited By ~ 44

Author(s):

Elisa d'Avila Cavalcanti-Oliveira ◽

Priscila Rufino da Silva ◽

Alessandra Peçanha Ramos ◽

Donato Alexandre Gomes Aranda ◽

Denise Maria Guimarães Freire

Keyword(s):

Soybean Oil ◽

Methyl Esters ◽

Reaction Medium ◽

Acid Catalyst ◽

Biodiesel Production ◽

Thermomyces Lanuginosus ◽

Molar Ratio ◽

Esterification Reaction ◽

Thermomyces Lanuginosus Lipase ◽

Niobic Acid

The process of biodiesel production by the hydroesterification route that is proposed here involves a first step consisting of triacylglyceride hydrolysis catalyzed by lipase from Thermomyces lanuginosus (TL 100L) to generate free fatty acids (FFAs). This step is followed by esterification of the FFAs with alcohol, catalyzed by niobic acid in pellets or without a catalyst. The best result for the enzyme-catalyzed hydrolysis was obtained under reaction conditions of 50% (v/v) soybean oil and 2.3% (v/v) lipase (25 U/mL of reaction medium) in distilled water and at 60∘C; an 89% conversion rate to FFAs was obtained after 48 hours of reaction. For the esterification reaction, the best result was with an FFA/methanol molar ratio of 1:3, niobic acid catalyst at a concentration of 20% (w/w FFA), and 200∘C, which yielded 92% conversion of FFAs to soy methyl esters after 1 hour of reaction. This study is exceptional because both the hydrolysis and the esterification use a simple reaction medium with high substrate concentrations.

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Enzymatic Synthesis of O-Methylated Phenophospholipids by Lipase-Catalyzed Acidolysis of Egg-Yolk Phosphatidylcholine with Anisic and Veratric Acids

Catalysts ◽

10.3390/catal10050538 ◽

2020 ◽

Vol 10 (5) ◽

pp. 538 ◽

Cited By ~ 3

Author(s):

Marta Okulus ◽

Anna Gliszczyńska

Keyword(s):

Egg Yolk ◽

Solvent System ◽

Biologically Active ◽

Molar Ratio ◽

Binary Solvent ◽

Molar Ratios ◽

Egg Yolk Phosphatidylcholine ◽

Screening Experiments ◽

Acidolysis Reaction ◽

System 1

Lipase-catalyzed acidolysis reactions of egg-yolk phosphatidylcholine (PC) with anisic (ANISA) and veratric (VERA) acids were investigated to develop a biotechnological method for the production of corresponding biologically active O-methylated phenophospholipids. Screening experiments with four commercially available immobilized lipases indicated that the most effective biocatalyst for the incorporation of ANISA into phospholipids was Novozym 435. None of the tested enzymes were able to catalyze the synthesis of PC structured with VERA. The effects of different solvents, substrate molar ratios, temperature, enzyme loading, and time of the reaction on the process of incorporation of ANISA into the phospholipids were evaluated in the next step of the study. The mixture of toluene/chloroform in the ratio 9:1 (v/v) significantly increased the incorporation of ANISA into PC. The acidolysis reaction was carried out using the selected binary solvent system, 1/15 substrate molar ratio PC/ANISA, 30% (w/w) enzyme load, and temperature of 50 °C afforded after 72 h anisoylated lysophosphatidylcholine (ANISA-LPC) and anisoylated phosphatidylcholine (ANISA-PC) in isolated yields of 28.5% and 2.5% (w/w), respectively. This is the first study reporting the production of ANISA-LPC and ANISA-PC via a one-step enzymatic method, which is an environmentally friendly alternative to the chemical synthesis of these biologically active compounds.

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Lipase Catalyzed Acidolysis for Efficient Synthesis of Phospholipids Enriched with Isomerically Pure cis-9,trans-11 and trans-10,cis-12 Conjugated Linoleic Acid

Catalysts ◽

10.3390/catal9121012 ◽

2019 ◽

Vol 9 (12) ◽

pp. 1012 ◽

Cited By ~ 1

Author(s):

Natalia Niezgoda ◽

Anna Gliszczyńska

Keyword(s):

Linoleic Acid ◽

Conjugated Linoleic Acid ◽

Biological Effects ◽

Reaction System ◽

Rhizomucor Miehei ◽

Egg Yolk ◽

Biologically Active ◽

Molar Ratio ◽

Active Compounds ◽

Cla Isomers

The production of phospholipid (PL) conjugates with biologically active compounds is nowadays an extensively employed approach. This type of phospholipids conjugates could improve bioavailability of many poorly absorbed active compounds such as isomers of conjugated linoleic acid (CLA), which exhibit versatile biological effects. The studies were carried out to elaborate an efficient enzymatic method for the synthesis of phospholipids with pure (>90%) cis-9,trans-11 and trans-10,cis-12 CLA isomers. For this purpose, three commercially available immobilized lipases were examined in respect to specificity towards CLA isomers in acidolysis of egg-yolk phosphatidylcholine (PC). Different incorporation rates were observed for the individual CLA isomers. Under optimal conditions: PC/CLA molar ratio 1:6; Rhizomucor miehei lipase loading 24% wt. based on substrates; heptane; DMF, 5% (v/v); water activity (aw), 0.11; 45 °C; magnetic stirring, 300 rpm; 48 h., effective incorporation (EINC) of CLA isomers into PC reached ca. 50%. The EINC of CLA isomers was elevated for 25–30% only by adding a water mimic (DMF) and reducing aw to 0.11 comparing to the reaction system performed at aw = 0.23. The developed method of phosphatidylcholine acidolysis is the first described in the literature dealing with isometrically pure CLA and allow to obtain very high effective incorporation.

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