Preparation of High-purity 1,3-Diacylglycerol Using Performance-enhanced Lipase Immobilized on Nanosized Magnetite Particles
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Early research on the nutritional value of 1,3-diacylglycerols (1,3-DAGs) has resulted in a significant interest in their synthesis. 1,3-DAGs can be produced chemically and biologically. In this work, a regioselective lipase from Rhizopus oryzae was efficiently immobilized on nanosized magnetite particles (NSM) in an oriented way, resulting in significant enhancement of activity. The specific hydrolytic and esterification activities of the immobilized enzyme were 1,660% and 260% of those of the free enzyme, respectively. The immobilized enzyme was then used to catalyze the esterification of oleic acid with glycerol in a solvent-free system for preparation of 1,3-DAG in a 1 L reactor. The catalytic process was studied in detail, the final concentration of 1,3-DAG reached >76% under the optimal condition when the molar ratio of oleic acid to glycerol was 2.8:1. The regioselectivities of free and immobilized enzyme were both >97%. The immobilized enzyme was reused for 55 cycles with only ∼30% activity loss at 30°C. The purity of 1,3-DAG was up to ∼95% (w/w) after a simple purification step with the recovery ratio ∼85%. This is the first report of efficient 1,3-DAG purification by neutralization without acyl migration.
KeywordsRhizopus oryzae lipase nanosized magnetite particles Fe3O4 immobilization esterification 1,3-diacylglycerols
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The authors thank the National Natural Science Foundation of China (Grant No. 21376215), National Basic Research Program of China (973, 2011CB710803), the National High-Tech Research and Development Program of China (863, 2012AA022302), and the National Natural Science Foundation cultivation project of Jining medical university (Grant no.JYP201704) for financial support. The authors declare no conflicts of interest.
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