Lipase‐catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)‐diricinolein

Abstract The objective of this study was to find the optimal parameters for lipase‐catalyzed methanolysis of triricinolein to produce 1,2(2,3)‐diricinolein. Four different immobilized lipases were tested, Candida antarctica type B (CALB), Rhizomucor miehei (RML), Pseudomonas cepacia (PCL), and Penic...

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Published in:Lipids
Main Authors: Turner, Charlotta, He, Xiaohua, Nguyen, Tasha, Lin, Jiann‐Tsyh, Wong, Rosalind Y., Lundin, Robert E., Harden, Leslie, McKeon, Thomas
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2003
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Online Access:http://dx.doi.org/10.1007/s11745-003-1179-5
https://onlinelibrary.wiley.com/doi/full/10.1007/s11745-003-1179-5
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spelling crwiley:10.1007/s11745-003-1179-5 2024-06-02T07:58:14+00:00 Lipase‐catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)‐diricinolein Turner, Charlotta He, Xiaohua Nguyen, Tasha Lin, Jiann‐Tsyh Wong, Rosalind Y. Lundin, Robert E. Harden, Leslie McKeon, Thomas 2003 http://dx.doi.org/10.1007/s11745-003-1179-5 https://onlinelibrary.wiley.com/doi/full/10.1007/s11745-003-1179-5 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Lipids volume 38, issue 11, page 1197-1206 ISSN 0024-4201 1558-9307 journal-article 2003 crwiley https://doi.org/10.1007/s11745-003-1179-5 2024-05-03T11:47:08Z Abstract The objective of this study was to find the optimal parameters for lipase‐catalyzed methanolysis of triricinolein to produce 1,2(2,3)‐diricinolein. Four different immobilized lipases were tested, Candida antarctica type B (CALB), Rhizomucor miehei (RML), Pseudomonas cepacia (PCL), and Penicillium roquefortii (PRL). n ‐Hexane and diisopropyl ether (DIPE) were examined as reaction media at three different water activities ( a w ), 0.11, 0.53, and 0.97. The consumption of triricinolein and the formation of 1,2(2,3)‐diricinolein, methyl ricinoleate, and ricinoleic acid were followed for up to 48 h. PRL gave the highest yield of 1,2(2,3)‐diricinolein. Moreover, this lipase showed the highest specificity for the studied reaction, i.e., high selectivity for the reaction with triricinolein but low for 1,2(2,3)‐diricinolein. Recoveries of 93 and 88% DAG were obtained using PRL in DIPE at a w of 0.11 and 0.53, respectively. Further, NMR studies showed that a higher purity of the 1,2(2,3)‐isomer vs. the 1,3‐isomer was achieved at higher a w (88% at a w =0.53), compared to lower a w (71% at a w =0.11). The DAG obtained was acylated by the DAG acyltransferase from Arabidopsis thaliana . Therefore, this enzymatic product is a useful enzyme substrate for lipid biosynthesis. Accordingly, the use of PRL in DIPE at a w 0.53 is considered optimal for the synthesis of 1,2(2,3)‐diricinolein from triricinolein. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Lipids 38 11 1197 1206
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description Abstract The objective of this study was to find the optimal parameters for lipase‐catalyzed methanolysis of triricinolein to produce 1,2(2,3)‐diricinolein. Four different immobilized lipases were tested, Candida antarctica type B (CALB), Rhizomucor miehei (RML), Pseudomonas cepacia (PCL), and Penicillium roquefortii (PRL). n ‐Hexane and diisopropyl ether (DIPE) were examined as reaction media at three different water activities ( a w ), 0.11, 0.53, and 0.97. The consumption of triricinolein and the formation of 1,2(2,3)‐diricinolein, methyl ricinoleate, and ricinoleic acid were followed for up to 48 h. PRL gave the highest yield of 1,2(2,3)‐diricinolein. Moreover, this lipase showed the highest specificity for the studied reaction, i.e., high selectivity for the reaction with triricinolein but low for 1,2(2,3)‐diricinolein. Recoveries of 93 and 88% DAG were obtained using PRL in DIPE at a w of 0.11 and 0.53, respectively. Further, NMR studies showed that a higher purity of the 1,2(2,3)‐isomer vs. the 1,3‐isomer was achieved at higher a w (88% at a w =0.53), compared to lower a w (71% at a w =0.11). The DAG obtained was acylated by the DAG acyltransferase from Arabidopsis thaliana . Therefore, this enzymatic product is a useful enzyme substrate for lipid biosynthesis. Accordingly, the use of PRL in DIPE at a w 0.53 is considered optimal for the synthesis of 1,2(2,3)‐diricinolein from triricinolein.
format Article in Journal/Newspaper
author Turner, Charlotta
He, Xiaohua
Nguyen, Tasha
Lin, Jiann‐Tsyh
Wong, Rosalind Y.
Lundin, Robert E.
Harden, Leslie
McKeon, Thomas
spellingShingle Turner, Charlotta
He, Xiaohua
Nguyen, Tasha
Lin, Jiann‐Tsyh
Wong, Rosalind Y.
Lundin, Robert E.
Harden, Leslie
McKeon, Thomas
Lipase‐catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)‐diricinolein
author_facet Turner, Charlotta
He, Xiaohua
Nguyen, Tasha
Lin, Jiann‐Tsyh
Wong, Rosalind Y.
Lundin, Robert E.
Harden, Leslie
McKeon, Thomas
author_sort Turner, Charlotta
title Lipase‐catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)‐diricinolein
title_short Lipase‐catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)‐diricinolein
title_full Lipase‐catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)‐diricinolein
title_fullStr Lipase‐catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)‐diricinolein
title_full_unstemmed Lipase‐catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)‐diricinolein
title_sort lipase‐catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)‐diricinolein
publisher Wiley
publishDate 2003
url http://dx.doi.org/10.1007/s11745-003-1179-5
https://onlinelibrary.wiley.com/doi/full/10.1007/s11745-003-1179-5
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Lipids
volume 38, issue 11, page 1197-1206
ISSN 0024-4201 1558-9307
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1007/s11745-003-1179-5
container_title Lipids
container_volume 38
container_issue 11
container_start_page 1197
op_container_end_page 1206
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