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Article: Lipase-catalyzed hydrolysis of TG containing acetylenic FA

TitleLipase-catalyzed hydrolysis of TG containing acetylenic FA
Authors
Issue Date2002
PublisherA O C S Press. The Journal's web site is located at http://www.aocs.org/press/lipids.htm
Citation
Lipids, 2002, v. 37 n. 10, p. 997-1006 How to Cite?
AbstractHydrolysis of symmetrical acetylenic TG of type AAA [viz., glycerol tri-(4-decynoate), glycerol tri-(6-octadecynoate), glycerol tri-(9-octadecynoate), glycerol tri-(10-undecynoate), and glycerol tri-(13-docosynoate)] in the presence of eight microbial lipases was studied. Novozyme 435 (Candida antarctica), an efficient enzyme for esterification, showed a significant resistance in the hydrolysis of glycerol tri-(9-octadecynoate) and glycerol tri-(13-docosynoate). Hydrolysis of acetylenic TG with Lipolase 100T (Humicola lanuginosa) was rapidly accomplished. Lipase PS-D (Pseudomonas cepacia) showed a fair resistance toward the hydrolysis of glycerol tri-(6-octadecynoate) only, which reflected its ability to recognize the Δ 6 positional isomer of 18:1. Lipase CCL (Candida cylindracea, syn. C. rugosa) and AY-30 (C. rugosa) were able to catalyze the release of 10-undecynoic acid and 9-octadecynoic acid from the corresponding TG, but less readily the 13-docosynoic acid in the case of glycerol tri-(13-docosynoate). The two lipases CCL and AY-30 were able to distinguish the small difference in structure of fatty acyl moieties in the TG substrate. To confirm this trend, three regioisomers of mixed acetylenic TG of type ABC (containing one each of Δ 6, Δ 9, and Δ 13 acetylenic FA in various positions) were prepared and hydrolyzed with CCL and AY-40. The results reconfirmed the observation that AY-30 and CCL were able to distinguish the slight differences in the molecular structure (position of the acetylenic bond and chain length) of the acyl groups in the TG during the hydrolysis of such TG substrates.
Persistent Identifierhttp://hdl.handle.net/10722/68342
ISSN
2015 Impact Factor: 1.892
2015 SCImago Journal Rankings: 0.795
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLie Ken Jie, MSFen_HK
dc.contributor.authorFu, Xen_HK
dc.contributor.authorLau, MMLen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2010-09-06T06:03:44Z-
dc.date.available2010-09-06T06:03:44Z-
dc.date.issued2002en_HK
dc.identifier.citationLipids, 2002, v. 37 n. 10, p. 997-1006en_HK
dc.identifier.issn0024-4201en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68342-
dc.description.abstractHydrolysis of symmetrical acetylenic TG of type AAA [viz., glycerol tri-(4-decynoate), glycerol tri-(6-octadecynoate), glycerol tri-(9-octadecynoate), glycerol tri-(10-undecynoate), and glycerol tri-(13-docosynoate)] in the presence of eight microbial lipases was studied. Novozyme 435 (Candida antarctica), an efficient enzyme for esterification, showed a significant resistance in the hydrolysis of glycerol tri-(9-octadecynoate) and glycerol tri-(13-docosynoate). Hydrolysis of acetylenic TG with Lipolase 100T (Humicola lanuginosa) was rapidly accomplished. Lipase PS-D (Pseudomonas cepacia) showed a fair resistance toward the hydrolysis of glycerol tri-(6-octadecynoate) only, which reflected its ability to recognize the Δ 6 positional isomer of 18:1. Lipase CCL (Candida cylindracea, syn. C. rugosa) and AY-30 (C. rugosa) were able to catalyze the release of 10-undecynoic acid and 9-octadecynoic acid from the corresponding TG, but less readily the 13-docosynoic acid in the case of glycerol tri-(13-docosynoate). The two lipases CCL and AY-30 were able to distinguish the small difference in structure of fatty acyl moieties in the TG substrate. To confirm this trend, three regioisomers of mixed acetylenic TG of type ABC (containing one each of Δ 6, Δ 9, and Δ 13 acetylenic FA in various positions) were prepared and hydrolyzed with CCL and AY-40. The results reconfirmed the observation that AY-30 and CCL were able to distinguish the slight differences in the molecular structure (position of the acetylenic bond and chain length) of the acyl groups in the TG during the hydrolysis of such TG substrates.en_HK
dc.languageengen_HK
dc.publisherA O C S Press. The Journal's web site is located at http://www.aocs.org/press/lipids.htmen_HK
dc.relation.ispartofLipidsen_HK
dc.titleLipase-catalyzed hydrolysis of TG containing acetylenic FAen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0024-4201&volume=37&issue=10&spage=997&epage=1006&date=2002&atitle=Lipase-catalyzed+hydrolysis+of+TG+containing+acetylenic+FAen_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s11745-006-0992-1en_HK
dc.identifier.pmid12530560-
dc.identifier.scopuseid_2-s2.0-0036818417en_HK
dc.identifier.hkuros76208en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036818417&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume37en_HK
dc.identifier.issue10en_HK
dc.identifier.spage997en_HK
dc.identifier.epage1006en_HK
dc.identifier.isiWOS:000180123800011-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLie Ken Jie, MSF=7004550473en_HK
dc.identifier.scopusauthoridFu, X=36805870500en_HK
dc.identifier.scopusauthoridLau, MML=7102344987en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK

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