dc.contributor.author |
O'Connor, Charmian |
en |
dc.contributor.author |
Bang, Kyong |
en |
dc.contributor.author |
Taylor, Carol |
en |
dc.contributor.author |
Brimble, MA |
en |
dc.date.accessioned |
2011-09-19T01:53:15Z |
en |
dc.date.issued |
2001 |
en |
dc.identifier.citation |
Journal of Molecular Catalysis B: Enzymatic 16 (3-4), 147-157, 2001 |
en |
dc.identifier.issn |
1873-3158 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/8070 |
en |
dc.description.abstract |
A selection of natural lipids, milk fat, cocoa butter and soybean oil, and three synthetic triglycerides 1,3-dipalmitoyl-2-oleoyl-rac-glycerol (POP), 1(3),2-palmitoyl-3(1)-oleoyl-rac-glycerol (PPO), and 1,3-dipalmitoyl-2-butyryl-rac-glycerol (PBP) were used as substrates for calf pregastric lipase (CPGL) catalysed hydrolysis at pH 6.5, 37.5 °C. CPGL preferentially releases short-chain fatty acids at the sn-3 position and unsaturated fatty acids during the hydrolysis of lipids containing long-chain fatty acids, and its activity increases with increasing unsaturation in the carbon chain of the long-chain fatty acids. The relative rate constants of hydrolysis were 1.56, 0.99, 0.73 h−1 for C4:0, C6:0, C8:0 esters, respectively, at sn-3; 0.0097, 0.0047 h−1 for the C16:0, C18:0 esters at sn-1,3, respectively; 0.0094 h−1 for the C18:1 ester at sn-2; and 0.0073, 0.0085, 0.012 h−1 for C18:1, C18:2, C18:3 esters, respectively, at sn-1,2,3. These last results confirmed that CPGL enzyme does not exhibit positional selectivity towards lipid substrates. The rate constant of hydrolysis was 1.14 h−1 for the C4:0 ester at sn-2. PBP was synthesised in four steps from commercially available glycerol as starting material. Glycerol was first selectively protected as a bis-silylether at the primary alcohol (sn-1,3) positions. The free alcohol at the sn-2 position was then esterified with butyric anhydride. The protecting groups at C1 and C3 were then removed, and the resultant hydroxyl groups esterified with palmitic acid. |
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dc.language |
EN |
en |
dc.publisher |
Elsevier |
en |
dc.relation.ispartofseries |
Journal of Molecular Catalysis B: Enzymatic |
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dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/1381-1177/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
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dc.subject |
calf pregastric lipase |
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dc.subject |
1,3-dipalmitoyl-2-butyryl-rac-glycerol |
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dc.subject |
lipid hydrolysis |
en |
dc.subject |
selectivity |
en |
dc.subject |
triacylglycerols |
en |
dc.subject |
CATALYZED HYDROLYSIS |
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dc.subject |
CHAIN-LENGTH |
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dc.subject |
TRIGLYCERIDES |
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dc.subject |
SPECIFICITY |
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dc.subject |
TEMPERATURE |
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dc.subject |
PH |
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dc.title |
Determining the regio- and typo-selectivity of calf pregastric lipase |
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dc.type |
Journal Article |
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dc.identifier.doi |
10.1016/S1381-1177(01)00052-2 |
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pubs.issue |
3-4 |
en |
pubs.begin-page |
147 |
en |
pubs.volume |
16 |
en |
dc.rights.holder |
Copyright: 2001 Elsevier Science B.V. |
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pubs.end-page |
157 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
4286 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Chemistry |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
pubs.record-created-at-source-date |
2010-09-01 |
en |