Optimization of diacylglycerol production by glycerolysis of fish oil catalyzed by Lipozyme TL IM with Tween 65

Blanco, Soeli Francisca Mazzini Monte; Santos, Joanna Silva; Feltes, Maria Manuela Camino; Dors, Gisanara; Licodiedoff, Silvana; Lerin, Lindomar Alberto; Oliveira, Débora de; Ninow, Jorge Luiz; Fúrigo, Agenor

doi:10.1007/s00449-015-1473-9

Cited by 15 publications

(6 citation statements)

References 37 publications

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“…Table 3 Significant variables presented p < 0.05. Coefficients with a positive sign indicate a synergic effect whereas negative coefficients indicate an antagonistic effect in the formation of MAG and DAG [24]. Moreover, the results presented show that any variation in the system significantly changes the conversion, statistically stating.…”

Section: Central Composite Rotatable Design (Ccrd)mentioning

confidence: 64%

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

Finco

Fiametti

Salva

et al. 2021

Preprint

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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.

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Section: Central Composite Rotatable Design (Ccrd)mentioning

confidence: 64%

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

Finco

Fiametti

Salva

et al. 2021

Preprint

View full text Add to dashboard Cite

show abstract

“…The conversion of TAG was in the range of 58 % to 98 %. Table 3 presents [24]. Moreover, the results presented show that any variation in the system significantly changes the conversion, statistically stating.…”

Section: Central Composite Rotatable Design (Ccrd)mentioning

confidence: 67%

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

Oliveira¹,

Finco²,

Fiametti³

et al. 2021

Preprint

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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.

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“…The type of lipase coupled with substrate manipulated the significance of enzyme concentration as both individual and cumulative effects were significant in immobilized CRL-catalyzed glycerolysis of olive oil [51], whereas only an individual effect was significant in Lipozyme TL IM-catalyzed glycerolysis of fish oil [52]. The enzyme concentration exhibited significant interactions with the substrate molar ratio mostly in transesterification [40,41], with temperature during esterification and transesterification [42,45], catalyzed by immobilized lipases with alcohol and vegetable oils as substrates.…”

Section: Statistical Significance Of Lipase Concentrationmentioning

confidence: 99%

Process Parameters Influence Product Yield and Kinetic Parameters in Lipase Catalysis

Bose,

Bhattacharjee,

Goswami

2023

ChemBioEng Reviews

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Effects of process parameters like enzyme concentration, concentration and type of substrate, pH, temperature, speed of agitation, and pressure on lipase catalysis are reviewed. The enzyme concentration controls its interfacial presence and consequently the rate of reaction. A change in substrate concentration alters lipase kinetics. Substrate‐lipase interaction varies with substrate type and pH. Water concentration and agitation affect the extent of interfacial area. Temperature impacts the rate and thermal denaturation of enzymes. Statistical optimization can solve the problem of controlling a variable's effect by other variables. Immobilization support and nonionic surfactant altered the significance of enzyme concentration. The lipase type controlled the impact of concentrations of enzyme, substrate, and water. The water content was important during lipase‐catalyzed hydrolysis and esterification. The mode of agitation influenced the significance of enzyme concentration and temperature. Time had a remarkable impact during hydrolysis. Temperature, substrate type, and chain length notably controlled kinetic parameters. This work paves the way for similar studies on other enzymes.

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Optimization of diacylglycerol production by glycerolysis of fish oil catalyzed by Lipozyme TL IM with Tween 65

Cited by 15 publications

References 37 publications

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

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

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

Process Parameters Influence Product Yield and Kinetic Parameters in Lipase Catalysis

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