Lipase-catalyzed hydrolysis of TG containing acetylenic FA
Hydrolysis 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 antar...
Published in: | Lipids |
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Format: | Article in Journal/Newspaper |
Language: | English |
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A O C S Press. The Journal's web site is located at http://www.aocs.org/press/lipids.htm
2002
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Online Access: | https://doi.org/10.1007/s11745-006-0992-1 http://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+FA http://hdl.handle.net/10722/68342 |
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ftunivhongkonghu:oai:hub.hku.hk:10722/68342 2023-05-15T13:54:24+02:00 Lipase-catalyzed hydrolysis of TG containing acetylenic FA Lie Ken Jie, MSF Chye, ML Fu, X Lau, MML 2002 https://doi.org/10.1007/s11745-006-0992-1 http://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+FA http://hdl.handle.net/10722/68342 eng eng A O C S Press. The Journal's web site is located at http://www.aocs.org/press/lipids.htm United States Lipids http://www.scopus.com/mlt/select.url?eid=2-s2.0-0036818417&selection=ref&src=s&origin=recordpage Lipids, 2002, v. 37 n. 10, p. 997-1006 doi:10.1007/s11745-006-0992-1 1006 76208 WOS:000180123800011 0024-4201 10 http://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+FA 12530560 eid_2-s2.0-0036818417 997 http://hdl.handle.net/10722/68342 37 Article 2002 ftunivhongkonghu https://doi.org/10.1007/s11745-006-0992-1 2023-01-14T15:13:24Z Hydrolysis 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. link_to_subscribed_fulltext Article in Journal/Newspaper Antarc* Antarctica University of Hong Kong: HKU Scholars Hub Rugosa ENVELOPE(-61.250,-61.250,-62.633,-62.633) Lipids 37 10 997 1006 |
institution |
Open Polar |
collection |
University of Hong Kong: HKU Scholars Hub |
op_collection_id |
ftunivhongkonghu |
language |
English |
description |
Hydrolysis 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. link_to_subscribed_fulltext |
format |
Article in Journal/Newspaper |
author |
Lie Ken Jie, MSF Chye, ML Fu, X Lau, MML |
spellingShingle |
Lie Ken Jie, MSF Chye, ML Fu, X Lau, MML Lipase-catalyzed hydrolysis of TG containing acetylenic FA |
author_facet |
Lie Ken Jie, MSF Chye, ML Fu, X Lau, MML |
author_sort |
Lie Ken Jie, MSF |
title |
Lipase-catalyzed hydrolysis of TG containing acetylenic FA |
title_short |
Lipase-catalyzed hydrolysis of TG containing acetylenic FA |
title_full |
Lipase-catalyzed hydrolysis of TG containing acetylenic FA |
title_fullStr |
Lipase-catalyzed hydrolysis of TG containing acetylenic FA |
title_full_unstemmed |
Lipase-catalyzed hydrolysis of TG containing acetylenic FA |
title_sort |
lipase-catalyzed hydrolysis of tg containing acetylenic fa |
publisher |
A O C S Press. The Journal's web site is located at http://www.aocs.org/press/lipids.htm |
publishDate |
2002 |
url |
https://doi.org/10.1007/s11745-006-0992-1 http://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+FA http://hdl.handle.net/10722/68342 |
long_lat |
ENVELOPE(-61.250,-61.250,-62.633,-62.633) |
geographic |
Rugosa |
geographic_facet |
Rugosa |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
Lipids http://www.scopus.com/mlt/select.url?eid=2-s2.0-0036818417&selection=ref&src=s&origin=recordpage Lipids, 2002, v. 37 n. 10, p. 997-1006 doi:10.1007/s11745-006-0992-1 1006 76208 WOS:000180123800011 0024-4201 10 http://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+FA 12530560 eid_2-s2.0-0036818417 997 http://hdl.handle.net/10722/68342 37 |
op_doi |
https://doi.org/10.1007/s11745-006-0992-1 |
container_title |
Lipids |
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37 |
container_issue |
10 |
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997 |
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1006 |
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1766260151223844864 |