Preparation of High-purity 1,3-Diacylglycerol Using Performanceenhanced Lipase Immobilized on Nanosized Magnetite Particles
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 pa...
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Published in | Biotechnology and bioprocess engineering pp. 326 - 336 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
한국생물공학회
01.04.2019
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Subjects | |
Online Access | Get full text |
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Summary: | 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 30ºC. 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. KCI Citation Count: 0 |
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ISSN: | 1226-8372 1976-3816 |
DOI: | 10.1007/s12257-018-0458-3 |