Byung Hee Kim and In-Hwan Kim contributed equally to this research
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Biocatalysts and Bioreactor Design
Synthesis of monoacylglycerol containing pinolenic acid via stepwise esterification using a cold active lipase
Article first published online: 27 JUL 2012
DOI: 10.1002/btpr.1596
Copyright © 2012 American Institute of Chemical Engineers (AIChE)
Additional Information
How to Cite
Pyo, Y.-G., Hong, S. I., Kim, Y., Kim, B. H. and Kim, I.-H. (2012), Synthesis of monoacylglycerol containing pinolenic acid via stepwise esterification using a cold active lipase. Biotechnol Progress, 28: 1218–1224. doi: 10.1002/btpr.1596
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Byung Hee Kim and In-Hwan Kim contributed equally to this research
Publication History
- Issue published online: 10 OCT 2012
- Article first published online: 27 JUL 2012
- Accepted manuscript online: 2 JUL 2012 11:44PM EST
- Manuscript Revised: 20 JUN 2012
- Manuscript Received: 7 APR 2012
Funded by
- Food Technology Development Program, Ministry for Food, Agriculture, Forestry and Fisheries, Republic of Korea
- Abstract
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Keywords:
- diacylglycerol;
- esterification;
- glycerol;
- monoacylglycerol;
- Penicillium camembertii;
- pinolenic acid
Abstract
High purity monoacylglycerol (MAG) containing pinolenic acid was synthesized via stepwise esterification of glycerol and fatty acids from pine nut oil using a cold active lipase from Penicillium camembertii as a biocatalyst. Effects of temperature, molar ratio, water content, enzyme loading, and vacuum on the synthesis of MAG by lipase-catalyzed esterification of glycerol and fatty acid from pine nut oil were investigated. Diacylglycerol (DAG) as well as MAG increased significantly when temperature was increased from 20 to 40°C. At a molar ratio of 1:1, MAG content decreased because of the significant increase in DAG content. Water has a profound influence on both MAG and DAG content through the entire course of reaction. The reaction rate increased significantly as enzyme loading increased up to 600 units. Vacuum was an effective method to reduce DAG content. The optimum temperature, molar ratio, water content, enzyme loading, vacuum, and reaction time were 20°C, 1:5 (fatty acid to glycerol), 2%, 600 units, 5 torr, and 24 h, respectively. MAG content further increased via lipase-catalyzed second step esterification at subzero temperature. P. camembertii lipase exhibited esterification activity up to −30°C. © 2012 American Institute of Chemical Engineers Biotechnol. Prog., 2012