Enzymatic synthesis of lysophosphatidic acid and phosphatidic acid
(1999) In Enzyme and Microbial Technology 24(10). p.651-658- Abstract
Immobilised 1,3-specific lipase from Rhizopus arrhizus was used as catalyst for the esterification of dl-glycero-3-phosphate and fatty acid or fatty acid vinyl ester in a solvent-free system. With lauric acid vinyl ester as acyl donor, a(w)<0.53 favored the synthesis of lysophosphatidic acid (1-acyl-rac-glycero-3-phosphate, LPA1) and the spontaneous acyl migration of the fatty acid on the molecule. Subsequent acylation by the enzyme resulted in high phosphatidic acid (1,2-diacyl-rac-glycero-3-phosphate, PA) formation and high total conversions (>95%). With oleic acid, maximum conversions of 55% were obtained at low water activities. Temperatures below melting point of the product favored precipitation and resulted in high final... (More)
Immobilised 1,3-specific lipase from Rhizopus arrhizus was used as catalyst for the esterification of dl-glycero-3-phosphate and fatty acid or fatty acid vinyl ester in a solvent-free system. With lauric acid vinyl ester as acyl donor, a(w)<0.53 favored the synthesis of lysophosphatidic acid (1-acyl-rac-glycero-3-phosphate, LPA1) and the spontaneous acyl migration of the fatty acid on the molecule. Subsequent acylation by the enzyme resulted in high phosphatidic acid (1,2-diacyl-rac-glycero-3-phosphate, PA) formation and high total conversions (>95%). With oleic acid, maximum conversions of 55% were obtained at low water activities. Temperatures below melting point of the product favored precipitation and resulted in high final conversion and high product ratio [LPA/(PA+LPA)]. Thus, LPA was the only product with lauric acid vinyl ester as acyl donor at 25°C. Increased substrate ratio (dl-glycero-3-phosphate/fatty acid) from 0.05 to 1 resulted in a higher ratio of LPA to PA formed, but a lower total conversion of dl-glycero-3-phosphate. Increased amounts of enzyme preparation did not result in higher esterification rates, probably due to high mass-transfer limitations. Copyright (C) 1999 Elsevier Science Inc. All rights reserved.
(Less)
- author
- Virto, Carmen LU ; Svensson, Ingemar LU and Adlercreutz, Patrick LU
- organization
- publishing date
- 1999-07-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- DL-glycero-3-phosphate, Esterification, Fatty acid vinyl ester, Lipase, Lysophosphatidic acid, Phosphatidic acid
- in
- Enzyme and Microbial Technology
- volume
- 24
- issue
- 10
- pages
- 8 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:0032926698
- ISSN
- 0141-0229
- DOI
- 10.1016/S0141-0229(98)00153-7
- language
- English
- LU publication?
- yes
- id
- 335e45c1-22ce-4997-8d82-44c598568d00
- date added to LUP
- 2019-06-20 16:02:06
- date last changed
- 2022-01-31 22:13:25
@article{335e45c1-22ce-4997-8d82-44c598568d00, abstract = {{<p>Immobilised 1,3-specific lipase from Rhizopus arrhizus was used as catalyst for the esterification of dl-glycero-3-phosphate and fatty acid or fatty acid vinyl ester in a solvent-free system. With lauric acid vinyl ester as acyl donor, a(w)<0.53 favored the synthesis of lysophosphatidic acid (1-acyl-rac-glycero-3-phosphate, LPA1) and the spontaneous acyl migration of the fatty acid on the molecule. Subsequent acylation by the enzyme resulted in high phosphatidic acid (1,2-diacyl-rac-glycero-3-phosphate, PA) formation and high total conversions (>95%). With oleic acid, maximum conversions of 55% were obtained at low water activities. Temperatures below melting point of the product favored precipitation and resulted in high final conversion and high product ratio [LPA/(PA+LPA)]. Thus, LPA was the only product with lauric acid vinyl ester as acyl donor at 25°C. Increased substrate ratio (dl-glycero-3-phosphate/fatty acid) from 0.05 to 1 resulted in a higher ratio of LPA to PA formed, but a lower total conversion of dl-glycero-3-phosphate. Increased amounts of enzyme preparation did not result in higher esterification rates, probably due to high mass-transfer limitations. Copyright (C) 1999 Elsevier Science Inc. All rights reserved.</p>}}, author = {{Virto, Carmen and Svensson, Ingemar and Adlercreutz, Patrick}}, issn = {{0141-0229}}, keywords = {{DL-glycero-3-phosphate; Esterification; Fatty acid vinyl ester; Lipase; Lysophosphatidic acid; Phosphatidic acid}}, language = {{eng}}, month = {{07}}, number = {{10}}, pages = {{651--658}}, publisher = {{Elsevier}}, series = {{Enzyme and Microbial Technology}}, title = {{Enzymatic synthesis of lysophosphatidic acid and phosphatidic acid}}, url = {{http://dx.doi.org/10.1016/S0141-0229(98)00153-7}}, doi = {{10.1016/S0141-0229(98)00153-7}}, volume = {{24}}, year = {{1999}}, }