Kinetics of solvent-free lipase-catalyzed glycerolysis of olive oil in surfactant system

A Valerio, RL Krüger, J Ninow… - Journal of Agricultural …, 2009 - ACS Publications
A Valerio, RL Krüger, J Ninow, FC Corazza, D de Oliveira, JV Oliveira, ML Corazza
Journal of Agricultural and Food Chemistry, 2009ACS Publications
This work reports experimental data and kinetic modeling of solvent-free glycerolysis of olive
oil using a commercial immobilized lipase (Novozym 435) in the presence of Triton X-100
surfactant for the production of monoacylglycerols (MAG) and diacylglycerols (DAG). The
experiments were performed in batch mode evaluating the effects of temperature (30− 70°
C), enzyme concentration (2.5− 18 wt%), Triton X-100 concentration (10− 20 wt%), and
glycerol to oil molar ratio (3: 1, 6: 1, and 9: 1). Experimental results showed that lipase …
This work reports experimental data and kinetic modeling of solvent-free glycerolysis of olive oil using a commercial immobilized lipase (Novozym 435) in the presence of Triton X-100 surfactant for the production of monoacylglycerols (MAG) and diacylglycerols (DAG). The experiments were performed in batch mode evaluating the effects of temperature (30−70 °C), enzyme concentration (2.5−18 wt %), Triton X-100 concentration (10−20 wt %), and glycerol to oil molar ratio (3:1, 6:1, and 9:1). Experimental results showed that lipase-catalyzed solvent-free glycerolysis with the addition of Triton X-100 might be a potential alternative route to conventional organic solvent methods, as good conversions were obtained with relatively low enzyme concentrations (9 wt %) in short reaction times (240 min). The glycerolysis and hydrolysis parallel reactions were considered with rate constants estimated by minimizing a maximum likelihood function. A very satisfactory agreement between experimental data and model results was obtained, thus allowing a better understanding of the reaction kinetics.
ACS Publications
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