Substrate Molar Ratio Research Articles

Lipase-catalyzed production of pyridoxine monolaurate in solvent-free bioreactor system

This study demonstrated that solvent-free gas bubbling system enhanced production efficiency of pyridoxine monolaurate in the esterification catalyzed by immobilized Candida antarctica lipase B (Lipozyme 435). Volumetric productivity in solvent-free gas bubbling system (41.24 mmol/L/h) was 3.7 and 2.1-fold higher than those in conventional organic solvent system (11.10 mmol/L/h) and solvent-free system (19.86 mmol/L/h) using magnetic stirring, respectively. Among the three bioreactor systems, solvent-free gas bubbling system provided the best reusability of the lipase retaining 94.45 % of initial activity for six batch reactions. In the bioreactor system, 5-O-lauroyl-pyridoxine was regioselectively produced with maximum production of 371.17 mmol/L at 70 °C and 0.10 of substrate molar ratio ([pyridoxine]/[lauric acid]) for 9 h. Pyridoxine monolaurate exhibited interfacial activity at oil-water interfaces, suggesting it had emulsifying properties. Pyridoxine monolaurate is expected to be applied as a multi-functional emulsifier with nutritional values to replace both small molecule emulsifiers and pyridoxine hydrochloride in fortified beverages.

Fabrication, characterization, and purification of nutraceutical diacylglycerol components from Camellia oil.

Converting triacylgycerols (TAGs) from edible oils and fats into structured diacylglycerols (DAGs) is meaningful for reducing obesity. Camellia oil, rich in linoleic acid, has the potential to form structured linoleic acid-1,3-diacylglycerol (LA-1,3-DAG) nutrients in the industry. In this research, the physicochemical properties of modified Camellia oil (MCO) by enzymatic esterification were analyzed by Gas Chromatography-Mass Spectrometry (GC-MS), Differential Scanning Calorimetry (DSC), High Performance Liquid Chromatography-Evaporative Light Scattering Detection (HPLC-ELSD), and Ultra Performance Liquid Chromatography-Tandem Mass Spectrometry (UPLC-MS/MS). The relationship between reaction conditions and the DAG compositions is disclosed using multiple factors. It is found that high constituents of DAG increase the melting and crystallization temperature of MCO, lipase Novozym 435 gives the best yield of targeted nutrients (DAG, 1,3-DAG, LA-DAG), and the mixture of lipases, Lipozyme TL IM and Lipozyme RM IM, shows a synergistic effect in the synthetic process of DAG. Subsequently, MCO containing 65.4% DAG, 54.7% LA-DAG, and 47.6% 1,3-DAG content at optimal conditions (2% enzyme dosage, 4 h reaction time, 2.4:1 substrate molar ratio, 25.8% t-butanol as solvent, 60°C temperature) has been obtained and purified using silica column to obtain the final DAG oil containing 96.1% DAG, 64.7% 1,3-DAG, and 78.4% LA-DAG. High constituents of structured DAG oil rich in LA-1,3-DAG can be obtained by enzymatic esterification for industrial production.

Ultrasound enhanced butyric acid-lauric acid designer lipid synthesis: Based on artificial neural network and changes in enzymatic structure

Ultrasound is a green technology for intensifying enzymatic reactions. In this study, an ultrasonic water bath with equipment parameters of 28 kHz, 1750.1 W/m2, 60% duty cycle was used to assist the synthesis of butyric acid-lauric acid designer lipid (BLDL), which was catalyzed by Lipozyme 435. A convincing three-layer feed-forward artificial neural network (ANN) model was established (R2 = 0.949, RMSE = 4.759, ADD = 7.329) to accurately predict the optimal parameters combination, which was described as 13.72 mL reaction volume, 15.49% enzyme loading, 0.253 substrate molar ratio (tributyrin/lauric acid), 56.58 °C reaction temperature and 120 min reaction time. The ultrasonic assistance increased actual butyric acid conversion rate by 11.38%, and also enhanced the consumption rate of tributyrin and lauric acid during the reaction. Meanwhile, the esterification activity of Lipozyme 435 was enhanced and its effectiveness up to 6 cycles. Structurally, ultrasound assistance significantly disrupted the secondary structure of the Lipozyme 435: reduced the content of α-helices, increased the content of β-sheet and β-turn. In addition, sonication caused an increase in crevice and micro-damage on the surface of the immobilized enzyme. In conclusion, low-intensity ultrasound at 28 kHz improved the synthesis efficiency of BLDL, which was scientifically predicted by ANN model, and the change of enzyme structure may be the vital reason for ultrasound enhanced reaction. However, the effect of ultrasound on immobilized enzymes’ activity needs to be further explored.

Enzymatic modification of triglycerides in conventional and surfactant-free microemulsions and in olive oil

Modification of the acylglycerol profile by interesterification of triacyglycerols (TAGs) can improve certain properties of food products. TAGs enriched in palmitic acid (PA) at the sn-2 position and in unsaturated fatty acids at the sn-1,3 position of the glycerol backbone are an important source of nutrients and energy for humans. In the present study, commercially available lipases have been used for the enzymatic interesterification of TAGs to form lipids containing PA and oleic acid (OA). Lipases A and B from Candida antarctica (CaL A and CaL B) and Thermomyces lanuginosus lipase (TLL) were tested in different environments from organic solvents to non-conventional systems such as w/o microemulsions (in the absence and presence of surfactants) and olive oil. The effects of reaction temperature, substrate molar ratio, and external energy were investigated. AOT microemulsions offered an excellent microenvironment for the interesterification reaction, while lecithin microemulsion affected TLL specificity. Surfactant-free microemulsions were also tested in terms of optimization of production process, however lower reaction yields were obtained. For the commercial immobilized CaL B, the ratio PA:triolein affected the reaction yield with the 2:1 ratio showing promising results in organic solvent environment. The main purpose of the present study was to elucidate the appropriate conditions for the enzymatic modification of olive oil. Several factors were tested such as substrates’ ratio, enzyme’s concentration, reaction temperature and external energy input. Overall, the ideal conditions for the formulation of the desired TAGs included the use of 50 mM free PA as substrate, 3 mg of immobilized CaL B/mL of olive oil while the reaction temperature was set at 40 °C and the duration was 72 h.

Enzymatic Synthesis of Diacylglycerol-Enriched Oil by Two-Step Vacuum-Mediated Conversion of Fatty Acid Ethyl Ester and Fatty Acid From Soy Sauce By-Product Oil as Lipid-Lowering Functional Oil.

Soy sauce by-product oil (SSBO), a by-product of the soy sauce production process, is the lack of utilization due to an abundance of free fatty acid (FFA) and fatty acid ethyl ester (EE). The utilization of low-cost SSBO to produce value-added diacylglycerol (DAG)-enriched oil and its applications are promising for the sustainability of the oil industry. The objective of this study was to utilize SSBO containing a high content of EE and FFA as raw material to synthesize DAG-enriched oil and to evaluate its nutritional properties in fish. Based on different behaviors between the glycerolysis of EE and the esterification of FFA in one-pot enzymatic catalysis, a two-step vacuum-mediated conversion was developed for the maximum conversions of EE and FFA to DAG. After optimization, the maximum DAG yield (66.76%) and EE and FFA conversions (96 and 93%, respectively) were obtained under the following optimized conditions: lipase loading 3%, temperature 38°C, substrate molar ratio (glycerol/FFA and EE) 21:40, a vacuum combination of 566 mmHg within the initial 10 h and 47 mmHg from the 10th to 14th hour. Further nutritional study in fish suggested that the consumption of DAG-enriched oil was safe and served as a functional oil to lower lipid levels in serum and liver, decrease lipid accumulation and increase protein content in body and muscle tissues, and change fatty acid composition in muscle tissues. Overall, these findings were vital for the effective utilization of SSBO resources and the development of future applications for DAG-enriched oil as lipid-lowering functional oil in food.

Mono- and dioleyl p-coumarate phenolipids and their antioxidant activity in a muscle food model system

Response surface methodology (RSM) was used to optimize the degree of esterification of p-coumaric acid to triolein via lipase-catalyzed acidolysis, and enzyme load, reaction time and mole ratio of substrates were selected as variables in the experimental design. The results showed that the model employed was highly sufficient for determining the effectiveness and interaction of three selected variables, enzyme load, reaction time and the mole ratio of substrates, on the dependent variable, the degree of esterification. Although the optimization point was not found in the selected range of the three variables, the steepest ascent analysis suggested that an increase of these three variables might lead to a stationary point. However, based on the limitations on increasing the range of tested variables, including possible oxidation of synthesized lipids and increased cost, the degree of esterification so yielded in the designed central composite design should be the one closest to the possible ideal optimized degree. The p-coumarates so produced exhibited varying antioxidant performance in the tested muscle food model, which could be explained by their different lipophilicity. Moreover, the potential health benefits of synthesized phenolic lipids have been discussed.Graphical

Enzymatic Synthesis and Molecular Modelling Studies of Rhamnose Esters Using Lipase from Pseudomonas stutzeri.

Rhamnolipids are becoming an important class of glycolipid biosurfactants. Herein, we describe for the first time the enzymatic synthesis of rhamnose fatty acid esters by the transesterification of rhamnose with fatty acid vinyl esters, using lipase from Pseudomonas stutzeri as a biocatalyst. The use of this lipase allows excellent catalytic activity in the synthesis of 4-O-acylrhamnose (99% conversion and full regioselectivity) after 3 h of reaction using tetrahydrofuran (THF) as the reaction media and an excess of vinyl laurate as the acyl donor. The role of reaction conditions, such as temperature, the substrates molar ratio, organic reaction medium and acyl donor chain-length, was studied. Optimum conditions were found using 35 °C, a molar ratio of 1:3 (rhamnose:acyldonor), solvents with a low logP value, and fatty acids with chain lengths from C4 to C18 as acyl donors. In hydrophilic solvents such as THF and acetone, conversions of up to 99–92% were achieved after 3 h of reaction. In a more sustainable solvent such as 2-methyl-THF (2-MeTHF), high conversions were also obtained (86%). Short and medium chain acyl donors (C4–C10) allowed maximum conversions after 3 h, and long chain acyl donors (C12–C18) required longer reactions (5 h) to get 99% conversions. Furthermore, scaled up reactions are feasible without losing catalytic action and regioselectivity. In order to explain enzyme regioselectivity and its ability to accommodate ester chains of different lengths, homology modelling, docking studies and molecular dynamic simulations were performed to explain the behaviour observed.

Catalytic activity of ethylbenzene with product selectivity by gold nanoparticles supported on zinc oxide.

The oxidation of ethylbenzene (EB) using tert-butyl hydroperoxide as the oxidizing agent was carried out in presence of gold nanoparticles (3 nm) supported on zinc oxide in acetonitrile solution. A higher selectivity towards acetophenone (ACP) as the major product, and a moderate selectivity towards other products such as 1-phenylethanol (PE), benzaldehyde (BZL), and benzoic acid (BzA) were observed using the prepared Au/ZnO nanocatalysts at 100 °C for 24 h. It is suggested the reaction produces an intermediate product, which is dimethylethyl-1-phenylethyl peroxide through a radical mechanism. A small amount of benzaldehyde was observed because benzaldehyde went autoxidation to form benzoic acid with the presence of oxidation agent of TBHP during reaction. The factors affecting the catalytic activity such as gold loading, calcination treatment at 300°C, type of solvent, reaction time, reaction temperature, oxidant to substrate molar ratio, catalyst weight, and solvent volume were studied. The gold nanoparticle catalyst synthesized by deposition precipitation method using urea was characterized by XRD, HRTEM, ATR-IR, XRF, and BET and offers a very selective reaction pathway for the oxidation of ethylbenzene.

Synthesis of partial glycerides rich in α-linolenic acid efficiently from silkworm pupa oil with immobilized lipase MAS1-H108A

In this paper the ability of immobilized lipase MAS1-H108A to prepare α-linolenic acid-rich partial glycerides was studied. The effects of different reaction conditions on the yield of Diacylglycerol (DAG) and Monoglyceride (MAG) were investigated, including substrate molar ratio, substrate concentration, temperature and lipase dosage. The highest yield (63.92% of MAG and 30.61% of DAG) was obtained when silkworm pupa oil/glycerol ratio of 1:3, lipase dosage was 50 U/g, substrate concentration was 40% (w/v), at 40 °C. Under the optimal conditions, the scale-up (50 times) and single-stage molecular distillation were carried out to separate DAG and MAG, the yield of MAG in the light phase was 99.18%, and the concentration of DAG in the heavy phase was 89.47%, α-linolenic acid in MAG and DAG accounted for 28.96% and 28.23%, respectively. The results can be shown that the immobilized lipase MAS1-H108A has excellent potential for enzymatic glycerolysis to prepare functional partial glycerides.

Enzymatic Production of Biologically Active 3-Methoxycinnamoylated Lysophosphatidylcholine via Regioselctive Lipase-Catalyzed Acidolysis.

Enzymatic acidolysis of egg-yolk phosphatidylcholine (PC) with 3-methoxycinnamic acid (3-OMe-CA) was investigated to produce biologically active 3-methoxycinnamoylated phospholipids. Four commercially available lipases were screened for their ability to incorporate 3-OMe-CA into PC. The results showed that Novozym 435 is the most effective biocatalyst for this process, while during the examination of organic solvents, heptane was found propriate reaction medium. The other reaction parameters including the substrate molar ratio, enzyme load and reaction time were designed using an experimental factorial design method. According to three-level-3-factor Box-Behnken model it was shown that all of studied parameters are crucial variables for the maximization of the synthesis of structured PLs. The optimum conditions derived via response surface methodology (RSM) were: 30% of lipase of the total weight of substrates, 1:15 molar ration of PC/3-OMe-CA and reaction time 4 days. The process of acidolysis performed on the increased scale at optimized parameters afforded two products. The major product, 3-methoxycinnamoylated lysophosphatidylcholine (3-OMe-CA-LPC) was isolated in high 48% yield, while 3-methoxycinnamoylated phosphatidylcholine (3-OMe-CA-PC) was produced in trace amount only in 1.2% yield. Obtained results indicate that presented biotechnological method of synthesis of 3-methoxycinnamoylated lysophosphatidylcholine is competitive to the previously reported chemical one.

Resolution of (R,S)-1-(4-methoxyphenyl)ethanol by lipase-catalyzed stereoselective transesterification and the process optimization.

An efficient lipase-catalyzed stereoselective transesterification reaction system was established for resolution of 1-(4-methoxyphenyl)ethanol (MOPE) enantiomers. A series of lipases were tested and compared. The immobilized lipase Novozym 40086 is selected as the best choice. The effects of organic solvent, acyl donor, time and temperature on substrate conversion (c), and optical purity of the remaining substrate (eeS ) were investigated. Response surface methodology and central composite design were employed to evaluate the effect of some important factors and to optimize the process. Under the optimized conditions including solvent of n-hexane, acyl donor of vinyl acetate, temperature of 35°C, substrate molar ratio of 1:6, enzyme dosage of 20 mg, and reaction time of 2.5 h, eeS of 99.87% with c of 56.71% is achieved. The use of alkane solvent and immobilized enzyme, the mild reaction conditions, and the reduced reaction time make the system promising in industrial application.

T enzymatic esterification of naringin and the properties of naringin esterified derivatization

As a kind of important natural compound with various physiological activities such as anti-oxidation, anti-inflammation, anti-aging, anti-cancer, anti-virus, etc, flavonoid had great application potential in food, cosmetics and pharmaceutical industries. However, the poor solubility limited their application. To solve this problem, one flavonoid glycoside, naringin, was esterified with lipase to improve its performance in the paper. Four fatty acids were selected as acyl donors to be esterified with naringin by single factor experiment, respectively. The results indicated that the optimal reaction conditions were the same: water activity was between 0.11 and 0.69, TLIM lipase was 50 mg/mL, acetone was used as the solvent, the molar ratio of substrate (naringin: fatty acid) was 1:10, and the substrates were first pretreated by ultrasound for 0.5 h, then reacted at 50 °C for 16 h. The conversion rates of naringin esterified with different fatty acids were all above 80.0%. Furtherly, the conversion rate of naringin was 93.9%, after the response surface experiment was carried out to optimize the lipase-catalyzed reaction conditions of naringin with palm oil. Lipophilicity and antioxidant ability of naringin esterified derivatives were measured. The results showed that the lipophilicity of naringin esterified derivatives was significantly higher than that of naringin. Although the free radical scavenging ability and reducing ability decreased by approximately 8% and 0.8%, respectively, the inhibiting oil peroxidation ability of naringin fatty acid esters were higher than that of naringin, which indicated that naringin esterified derivatives have the potential to become fat-soluble antioxidants.

Drug-Free Liposomes Containing Mannosylated Ligand for Liver-Targeting: Synthetic Optimization, Liposomal Preparation, and Bioactivity Evaluation.

This research was performed to optimize the enzymatic synthesis of mannosylated ligand with which to prepare mannosy-lated liposomes and investigate their bioactivity. Based on single-factor studies, lipase dose, substrate molar ratio (diester lauric diacid-cholesterol to mannose) and temperature were identified as significant parameters, and optimal reaction conditions were determined through response surface methodology (RSM) with central composite design. The optimum operating parameters, 61.23 mg of lipase, a substrate molar ratio of 5.36, and 56.64 °C temperature offered a predicted yield (71.11%) which was consistent with the actual yield (69.08%). Drug-free mannosylated liposomes were prepared film-dispersion. The characterizations of these liposomes showed that mannosylated liposomes were well-dispersible spherical particles with an average particle size of 142.3 nm, the polydispersity index of 0.16, and a zeta potential of -19.8 mV. Pyrogen examination, hemolytic studies and cytotoxicity assays revealed no substantial safety concern for drug-free mannosylated liposomes. Cellular uptake efficiency of mannosylated liposomes by HepG2 cells was significantly higher than that of unmodified liposomes, demonstrating that mannosylated ligands have a positive effect on liver targeting. Overall, mannosylated liposomes could be active drug delivery system for combatting the therapy of hepatic diseases.

Enzymatic acylation of lutein with a series of saturated fatty acid vinyl esters and the thermal stability and anti-lipid oxidation properties of the acylated derivatives.

Lutein was enzymatically acylated with saturated fatty acid vinyl esters of different lengths of carbon chain (C6 -C14 ) under the action of Candida antarctica lipase B (Novozyme 435). The acylation reaction was optimized by considering substrate molar ratio, reaction solvent, type of enzyme, and reaction time. The highest yield (88%) was obtained using the Novozyme 435 to catalyze the acylation reaction of lutein and vinyl decanoate (lutein/vinyl decanoate molar ratio of 1/10) for 16 h in methyl tert-butyl ether. Ten lutein esters were synthesized, isolated, and purified, which were characterized by Fourier-transform infrared spectroscopy, high-resolution mass spectrometry, and nuclear magnetic resonance spectroscopy. We found that the acylation of lutein improved its antioxidant capacity in lipid system and thermal stability. Our study extended the potential application of lutein in lipophilic food, cosmetic, and pharmaceutical industries. Practical Application: Enzyme acylation of lutein improved its antioxidant capacity in lipid system and thermal stability, extended its potential application in food, cosmetic, and pharmaceutical industries. In addition, our study also provided a new perspective and cognition for the further development and utilization of lutein.

Highly efficient synthesis of chlorogenic oleate using acyl chloride method

In this study, chlorogenic oleate (CGO) was efficiently synthesized through acylation of chlorogenic acid (CGA) and oleoyl chloride. The effects of substrate molar ratio, adding method of oleoyl chloride, reaction time, reaction temperature, and molar ratio of CGA to triethylamine on the CGA conversion were investigated. The results indicated that the optimal conditions were as follows: molar ratio of CGA to oleoyl chloride 1:1.5, adding method of oleoyl chloride 4 aliquots, reaction time 20 min, reaction temperature 25 °C, molar ratio of CGA to triethylamine 1:1.5. Under the conditions, the CGA conversion was up to 76.62%. The crude product was then purified by solvent extraction, and the purity of CGO was 94.96%. The structure of CGO was identified by FTIR, HPLC-MS and NMR.

One-Pot Synthesis of 4H-Pyrano[3,2-c]coumarin Derivatives Catalyzed by Deep Eutectic Solvent

Abstract4H-Pyrano[3,2-c]coumarin derivatives are an important class of pharmaceutical compounds that are expensive to prepare by previously reported methods. An efficient and green method was developed to obtain these derivatives using the deep eutectic solvent (DES) zinc chloride/acetamide (n:n = 1:4), which acted as both the catalyst and the solvent for the reaction. An aromatic aldehyde, 4-hydroxycoumarin, and cyanoacetate were used as the substrates. The DES, substrate molar ratio, diluent type, temperature, and reaction time were optimized to obtain the 4H-pyrano[3,2-c]coumarin derivatives from a range of aromatic aldehydes in a single step in moderate to high yields and under mild reaction conditions.

Synthesis and oxidative stability of monoacylglycerols containing polyunsaturated fatty acids by enzymatic glycerolysis in a solvent-free system

Monoacylglycerols (MAG) containing polyunsaturated fatty acids (PUFA) have been synthesized by glycerolysis of anchovy oil using Lipozyme RM-IM in a solvent-free system. The experimental conditions, reaction temperature, substrate molar ratio (glycerol/triacylglycerol, Gly/TAG) and enzyme concentration were studied. A response surface methodology was employed to analyze the effect of the individual variables on MAG production and oxidative stability with respect to induction time. The operating conditions that simultaneously optimized MAG yields and oxidative stability were a reaction temperature of 40 °C, a Gly/TAG molar ratio of 2:1 and 6% enzyme load. The yield obtained was 20.34% of MAG (with 12.12% of 2-MAG) and an induction time of 1.88 h.

Bimetallic MOF-Derived Synthesis of Cobalt-Cerium Oxide Supported Phosphotungstic Acid Composites for the Oleic Acid Esterification

The impregnation of phosphotungstic acid (HPW) with porous cobalt-cerium oxide (HPW@CoCeO) has been prepared by pyrolysis of CoCe-MOF and used for the production of methyl oleate from oleic acid and methanol. FTIR, XRD, SEM, TEM, N2 adsorption/desorption, and NH3-TPD were characterized for the prepared composites. Simultaneously, the effects of reaction time, substrate molar ratio, temperature, and catalyst loading on catalytic activity were highlighted, and the conversion of 67.2% was reached after 4 h at 60°C. Importantly, HPW@CoCeO was reusabe and reused more than eight times, and the oleic acid conversion could be maintained at 61.8% without significant activity loss. Thus, the HPW@CoCeO composite could be used as acid catalysts for sustainable energy production.

Complexation in situ of 1-methylpiperidine, 1,2-dimethylpyrrolidin, and 1,2-dimethylpiperidine with rhodium(II) tetracarboxylates: Nuclear magnetic resonance spectroscopy, chiral recognition, and density functional theory studies.

Complexation in situ of 1-methylpiperidine, racemic 1,2-dimethylpyrrolidin, and racemic 1,2-dimethylpiperidine with rhodium(II) tetracarboxylates in chloroform was studied by 1 H and 13 C nuclear magnetic resonance (NMR) spectroscopy and density functional theory (DFT) methods. As substrates, three dirhodium(II) compounds were applied, tetraacetate, tetrakistrifluoroacetate, and a derivative of optically pure Mosher's acid. Due to conformational flexibility, free and complexed ligands can adopt potentially various conformations. The NMR titration experiments revealed the subsequent formation of 1:1 and 1:2 complexes, depending on the molar ratio of substrate to ligand. Conformations of free and complexed ligands were examined by the comparison of experimental and DFT gauge-independent atomic orbital (GIAO) calculated chemical shifts and by the analysis of the internal energy of the compounds. For some ligand and substrate combinations, a mixture of complexes differing in ligand conformations was formed. Complexes of Mosher's acid derivative of rhodium(II) with racemic 1,2-dimethylpyrrolidin and 1,2-dimethylpiperidine exhibited NMR chiral recognition phenomenon, manifested by splitting of signals in 13 C NMR and 1 H,13 C HSQC spectra.

Soybean oil-based monoacylglycerol synthesis using bio-compatible amino acid ionic liquid as a catalyst at low temperature

Monoacylglycerol (MAG) from edible oil is one kind of green and safe food additive. This project mainly focused on a nontoxic and biodegradable catalyst, amino acid-based ionic liquids (AAILs), for the glycerolysis of soybean oil triacylglycerol (TAG) to prepare MAG at low temperature. Seven AAILs, from arginine, lysine, histidine, tryptophan, or glutamic acid and choline hydroxide, tetramethylhydroxide ammonium, or tetrabutylammonium hydroxide, were successfully synthesized in this work. The effects of substrate ratio, AAIL load, temperature, and reaction time on AAIL-catalyzed the glycerolysis of soybean oil were evaluated. Moreover, the activation energy of MAG formation was explored and reaction mechanism was also proposed. Finally, reaction conditions were optimized by response surface methodology. Results showed that, among all tested AAILs, [TMA][Arg] prepared by arginine (Arg) and tetramethylhydroxide ammonium (TMAOH) showed the outstanding catalytic performance for the glycerolysis of soybean oil. The maximum MAG yield (64.89 ± 1.26%) and TAG conversion (86.31 ± 1.68%) were achieved under the optimized conditions: 105 °C, 0.5 h, [TMA][Arg] load 10%, and substrate molar ratio 1:2 (soybean oil/glycerol). Moreover, the activation energies of MAG formation and TAG conversion were 44.22 kJ/mol and 37.58 kJ/mol, respectively.