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Lipase specificity towards eicosapentaenoic acid and docosahexaenoic acid depends on substrate structure.

Lyberg, Ann-Marie LU and Adlercreutz, Patrick LU (2008) In Biochimica et Biophysica Acta - Proteins and Proteomics 1784(2). p.343-350
Abstract
The fatty acid specificity of five lipases towards eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) was evaluated in the hydrolysis of fish oil, squid oil and a model system. The model system contained methyl esters of EPA, DHA and palmitic acid. All the investigated lipases discriminated against both EPA and DHA more in the model system than in the natural oils. Thus both EPA and DHA were more easily hydrolysed from a glyceride than from a methyl ester. In the model system, the lipase from Candida rugosa showed the highest discrimination against DHA, while the lipases from Pseudomonas fluorescens and Pseudomonas cepacia discriminated against EPA the most. In a glyceride, the fatty acid specificity of lipases towards EPA and DHA... (More)
The fatty acid specificity of five lipases towards eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) was evaluated in the hydrolysis of fish oil, squid oil and a model system. The model system contained methyl esters of EPA, DHA and palmitic acid. All the investigated lipases discriminated against both EPA and DHA more in the model system than in the natural oils. Thus both EPA and DHA were more easily hydrolysed from a glyceride than from a methyl ester. In the model system, the lipase from Candida rugosa showed the highest discrimination against DHA, while the lipases from Pseudomonas fluorescens and Pseudomonas cepacia discriminated against EPA the most. In a glyceride, the fatty acid specificity of lipases towards EPA and DHA was affected by the positional distribution of the fatty acids and the glyceride structure due to the regiospecificity and triglyceride specificity of the lipase. In the oils, the Pseudomonas lipases also discriminated against EPA the most, while DHA was initially discriminated the most by the lipase from Thermomyces lanuginosus. However, after longer reaction times the enrichment of DHA in the glyceride fraction of the oils was greatest for the lipase from C. rugosa. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Docosahexaenoic acid, Competitive factor, Hydrolysis, Eicosapentaenoic acid, Lipase
in
Biochimica et Biophysica Acta - Proteins and Proteomics
volume
1784
issue
2
pages
343 - 350
publisher
Elsevier
external identifiers
  • pmid:18067872
  • wos:000253353600010
  • scopus:38549167394
ISSN
1570-9639
DOI
10.1016/j.bbapap.2007.11.003
language
English
LU publication?
yes
id
aa701343-ef8c-4d70-b265-ae9de0b5f9e5 (old id 1035459)
date added to LUP
2008-12-01 11:38:49
date last changed
2017-11-05 03:59:51
@article{aa701343-ef8c-4d70-b265-ae9de0b5f9e5,
  abstract     = {The fatty acid specificity of five lipases towards eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) was evaluated in the hydrolysis of fish oil, squid oil and a model system. The model system contained methyl esters of EPA, DHA and palmitic acid. All the investigated lipases discriminated against both EPA and DHA more in the model system than in the natural oils. Thus both EPA and DHA were more easily hydrolysed from a glyceride than from a methyl ester. In the model system, the lipase from Candida rugosa showed the highest discrimination against DHA, while the lipases from Pseudomonas fluorescens and Pseudomonas cepacia discriminated against EPA the most. In a glyceride, the fatty acid specificity of lipases towards EPA and DHA was affected by the positional distribution of the fatty acids and the glyceride structure due to the regiospecificity and triglyceride specificity of the lipase. In the oils, the Pseudomonas lipases also discriminated against EPA the most, while DHA was initially discriminated the most by the lipase from Thermomyces lanuginosus. However, after longer reaction times the enrichment of DHA in the glyceride fraction of the oils was greatest for the lipase from C. rugosa.},
  author       = {Lyberg, Ann-Marie and Adlercreutz, Patrick},
  issn         = {1570-9639},
  keyword      = {Docosahexaenoic acid,Competitive factor,Hydrolysis,Eicosapentaenoic acid,Lipase},
  language     = {eng},
  number       = {2},
  pages        = {343--350},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta - Proteins and Proteomics},
  title        = {Lipase specificity towards eicosapentaenoic acid and docosahexaenoic acid depends on substrate structure.},
  url          = {http://dx.doi.org/10.1016/j.bbapap.2007.11.003},
  volume       = {1784},
  year         = {2008},
}