Determining the regio- and typo-selectivity of calf pregastric lipase

ResearchSpace/Manakin Repository

Show simple item record

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. en
dc.language EN en
dc.publisher Elsevier en
dc.relation.ispartofseries Journal of Molecular Catalysis B: Enzymatic en
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 en
dc.subject calf pregastric lipase en
dc.subject 1,3-dipalmitoyl-2-butyryl-rac-glycerol en
dc.subject lipid hydrolysis en
dc.subject selectivity en
dc.subject triacylglycerols en
dc.subject CATALYZED HYDROLYSIS en
dc.subject CHAIN-LENGTH en
dc.subject TRIGLYCERIDES en
dc.subject SPECIFICITY en
dc.subject TEMPERATURE en
dc.subject PH en
dc.title Determining the regio- and typo-selectivity of calf pregastric lipase en
dc.type Journal Article en
dc.identifier.doi 10.1016/S1381-1177(01)00052-2 en
pubs.issue 3-4 en
pubs.begin-page 147 en
pubs.volume 16 en
dc.rights.holder Copyright: 2001 Elsevier Science B.V. en
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


Full text options

Full text for this item is not available in ResearchSpace.

Find Full text

This item appears in the following Collection(s)

Show simple item record

Share

Search ResearchSpace


Advanced Search

Browse