Akanbi_2014_Food.Chem_160_61

Reference

Title : Pancreatic lipase selectively hydrolyses DPA over EPA and DHA due to location of double bonds in the fatty acid rather than regioselectivity - Akanbi_2014_Food.Chem_160_61
Author(s) : Akanbi TO , Sinclair AJ , Barrow CJ
Ref : Food Chem , 160 :61 , 2014
Abstract :

The enzymatic hydrolysis of canola, anchovy and seal oils with different types and amounts of polyunsaturated fatty acids was measured using porcine pancreatic lipase (PPL) to establish the fatty acid selectivity of PPL. Substrates were subjected to the same conditions of hydrolysis, with percent hydrolysis monitored using Iatroscan and fatty acid selectivity monitored using gas chromatography (GC). Regardless of their distribution on the glycerol backbone, as monitored by (13)C nuclear magnetic resonance (NMR), alpha-linolenic acid (ALA) and docosapentaenoic acid (DPA) were rapidly cleaved by PPL while eicosapentaenoic acid (EPA), docosahexaenoic acid (DHA) and stearidonic acid (STA) were hydrolysed more slowly. Results show that PPL preferentially hydrolyses ALA and DPA over EPA, DHA and STA, and this selectivity is due to fatty acid rather than regioselectivity. The primary structural factor associated with resistance to PPL appears to be the distance of the first double bond from the ester linkage being hydrolysed.

PubMedSearch : Akanbi_2014_Food.Chem_160_61
PubMedID: 24799209

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Citations formats

Akanbi TO, Sinclair AJ, Barrow CJ (2014)
Pancreatic lipase selectively hydrolyses DPA over EPA and DHA due to location of double bonds in the fatty acid rather than regioselectivity
Food Chem 160 :61

Akanbi TO, Sinclair AJ, Barrow CJ (2014)
Food Chem 160 :61