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