Kinetic study of liquid lipase-catalyzed glycerolysis of olive oil using Lipozyme TL 100L

Monoacylglycerol (MAG) and diacylglycerol (DAG) are two natural components found in most edible oils and fats. Conventional synthesis of MAG and DAG is usually conducted by glycerolysis of triacylglycerol (TAG) at high temperatures (above 200 °C) in the presence of an alkaline catalyst. In this work, the synthesis of MAG and DAG using enzymatic glycerolysis of olive oil was investigated using Tween 80 as surfactant, n-butanol as co-surfactant and the novel lipase in free/liquid formulation Lipozyme TL 100L as catalyst. Experimental design was used to evaluate the effect of enzyme load and reaction temperature on the feedstock conversion. Enzyme load and system temperature were significant variables in the statistical design and the best condition was found at 35 °C, 7.5 vol% of Lipozyme TL 100 and glycerol to oil molar ratio of 2:1 with conversion of TAG at approximately 98 % after 2 h of process. A mathematical model based on the Ping-Pong Bi-Bi mechanism was used to describe the reaction kinetics. The model adequately described the behavior of the system and can be a useful tool for the design of reactors in larger scales.

Kinetic study of liquid lipase-catalyzed glycerolysis from olive oil using Lipozyme TL 100L

Monoacylglycerol (MAG) and diacylglycerol (DAG) are two natural components found in most edible oils and fats. Conventional synthesis of MAG and DAG is usually conducted by glycerolysis of triacylglycerol (TAG) at high temperatures (above 200 °C) in the presence of an alkaline catalyst. In this work, the synthesis of MAG and DAG using enzymatic glycerolysis of olive oil was investigated using Tween 80 as surfactant, n-butanol as co-surfactant and the novel lipase in free/liquid formulation Lipozyme TL 100L as catalyst. Experimental design was used to evaluate the effect of enzyme load and reaction temperature on the feedstock conversion. Enzyme load and system temperature were significant variables in the statistical design and the best condition was found at 35 °C, 7.5 vol% of Lipozyme TL 100 and 2:1 molar ratio (glycerolysis:oil) with conversion of TAG at approximately 98 % after 2 h of process. A mathematical model based on the Ping-Pong Bi-Bi mechanism was used to describe the reaction kinetics. The model adequately described the behavior of the system and can be a useful tool for the design of reactors in larger scales.

Kinetic Study of Liquid Lipase-catalyzed Glycerolysis From Olive Oil Using Lipozyme TL 100L

Monoacylglycerol (MAG) and diacylglycerol (DAG) are two natural components found in most edible oils and fats. Conventional synthesis of MAG and DAG is usually conducted by glycerolysis of triacylglycerol (TAG) at high temperatures (above 200 °C) in the presence of an alkaline catalyst. In this work, the synthesis of MAG and DAG using enzymatic glycerolysis of olive oil was investigated using Tween 80 as surfactant, n-butanol as co-surfactant and the novel lipase in liquid formulation Lipozyme TL 100L as catalyst. Experimental design was used to evaluate the effect of enzyme load and reaction temperature on the feedstock conversion. Enzyme load and system temperature were significant variables in the statistical design and the best condition was found at 35 °C, 7.5 vol% of Lipozyme TL 100 and 2:1 molar ratio (glycerolysis:oil) with conversion of TAG at approximately 98 % after 2 h of process. A mathematical model based on the Ping-Pong Bi-Bi mechanism was used to describe the reaction kinetics. The model adequately described the behavior of the system and can be a useful tool for the design of reactors in larger scales.

Immobilization of Eversa® Transform via CLEA Technology Converts It in a Suitable Biocatalyst for Biolubricant Production Using Waste Cooking Oil

The performance of the previously optimized magnetic cross-linked enzyme aggregate of Eversa (Eversa-mCLEA) in the enzymatic synthesis of biolubricants by transesterification of waste cooking oil (WCO) with different alcohols has been evaluated. Eversa-mCLEA showed good activities using these alcohols, reaching a transesterification activity with isoamyl alcohol around 10-fold higher than with methanol. Yields of isoamyl fatty acid ester synthesis were similar using WCO or refined oil, confirming that this biocatalyst could be utilized to transform this residue into a valuable product. The effects of WCO/isoamyl alcohol molar ratio and enzyme load on the synthesis of biolubricant were also investigated. A maximum yield of around 90 wt.% was reached after 72 h of reaction using an enzyme load of 12 esterification units/g oil and a WCO/alcohol molar ratio of 1:6 in a solvent-free system. At the same conditions, the liquid Eversa yielded a maximum ester yield of only 34%. This study demonstrated the great changes in the enzyme properties that can be derived from a proper immobilization system. Moreover, it also shows the potential of WCO as a feedstock for the production of isoamyl fatty acid esters, which are potential candidates as biolubricants.

OPTIMIZATION OF FATTY ACID GENERATION USING PARAMETRIC ANALYSIS

The objective of this study is to optimize the different parameters to carry out analysis of fatty acids. A kinetic was observed for first order enzymatic hydrolysis of flax seed methyl ester was carried out by using Rhizomucor michei. In this study the analysis of hydrolysis was carried out by varying the temperature (30-40oC) and enzyme load (2-5%). The optimal condition were found to temperature 50oC, 6h reaction time, buffer to flax seed methyl ester ratio 1.5:1(v/w) and 4% enzyme load to achieve a maximum hydrolysis conversion of 97.56%. The effect of temperature on the reaction rate constant and equilibrium constant has been determined using Arrhenius equation. The heat of reaction was found 14.516 KJ/mol. Taguchi's design of experiment L16 and L9 orthogonal array was performed to optimize hydrolysis reaction conditions. Rate of reaction, effect of temperature, enzyme modifier, pH and oil to buffer ratio were considered as a primary influencing parameters which effects the percentage of hydrolysis and fatty acid formed. From the analysis of variance, the influencing parameters on production of fatty acid were reaction time and enzyme modifier. The predicted conversion was found in good rectification with experimental values having R2=0.9945 and R2=0.983. Maximum fatty acid formed was 98.76% from methyl ester and 98.92% from oil.

Development and Optimization of Lipase-Catalyzed Synthesis of Phospholipids Containing 3,4-Dimethoxycinnamic Acid by Response Surface Methodology

The interesterification reaction of egg-yolk phosphatidylcholine (PC) with ethyl ester of 3,4-dimethoxycinnamic acid (E3,4DMCA) catalyzed by Novozym 435 in hexane as a reaction medium was shown to be an effective method for the synthesis of corresponding structured O-methylated phenophospholipids. The effects of substrate molar ratios, time of the reaction and enzyme load on the process of incorporation of 3,4DMCA into PC were evaluated by using the experimental factorial design of three factors and three levels. The results showed that a substrate molar ratio is a crucial variable for the maximization of the synthesis of 3,4-dimethoxycinnamoylated phospholipids. Under optimized parameters of 1/10 substrate molar ratio PC/E3,4DMCA, enzyme load 30% (w/w), hexane as a medium and incubation time of 3 days, the incorporation of aromatic acid into phospholipid fraction reached 21 mol%. The modified phosphatidylcholine (3,4DMCA-PC) and modified lysophosphatidylcholine (3,4DMCA-LPC) were obtained in isolated yields of 3.5% and 27.5% (w/w), respectively. The developed method of phosphatidylcholine interesterification is the first described in the literature dealing with 3,4DMCA and allows us to obtain new O-methylated phenophospholipids with potential applications as food additives or nutraceuticals with pro-health activity.

Enhanced Ricinoleic Acid Preparation Using Lipozyme TLIM as a Novel Biocatalyst: Optimized by Response Surface Methodology

Ricinoleic acid (RA) is an important raw material for plasticizers, emulsifiers, and nanomaterials. In this work, a green and efficient method was developed for RA production. Results showed that Lipozyme TLIM can be used as a novel biocatalyst to catalyze the hydrolysis of castor oil (CO) for RA preparation. Response surface methodology (RSM) was used to evaluate and optimize the effects of reaction variables on the hydrolysis of CO. Reaction conditions were optimized as follows: 41.3 °C, enzyme load 8.9%, 39.2 h, and 40:1 molar ratio of water to oil. Under these optimized reaction variables, the maximum hydrolysis ratio of CO (96.2 ± 1.5%) was obtained. The effect of hydrolysis variables on the reaction was as follows: enzyme load > hydrolysis time > temperature. In conclusion, this is a green, simple, and efficient method for RA preparation and can provide a good alternative method for RA industrial production.