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Kinetic study of liquid lipase‐catalyzed glycerolysis of olive oil using Lipozyme TL 100L
Author(s) -
Finco George F.,
Fiametti Karina G.,
Lobo Viviane da Silva,
da Silva Edson A.,
Palú Fernando,
Wancura João H. C.,
Rodrigues Maria L. F.,
Valério Alexsandra,
Oliveira José Vladimir
Publication year - 2022
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1002/aocs.12593
Subject(s) - chemistry , lipase , monoacylglycerol lipase , catalysis , glycerol , pulmonary surfactant , diacylglycerol kinase , chromatography , glyceride , organic chemistry , kinetics , diglyceride , monoglyceride , enzyme , fatty acid , biochemistry , endocannabinoid system , receptor , protein kinase c , physics , quantum mechanics
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 100L and glycerol to oil volumetric 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.