Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids
LML-type structured lipids are one type of medium- and long-chain triacylglycerols. LML was synthesized using immobilized Talaromyces thermophilus lipase (TTL)-catalyzed interesterification of tricaprylin and ethyl linoleate. The resin AB-8 was chosen, and the lipase/support ratio was determined to...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Springer
2019
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| Online Access: | http://psasir.upm.edu.my/id/eprint/80148/1/Immobilized%20Talaromyces%20thermophilus%20lipase%20as%20an%20efficient%20catalyst%20for%20the%20production%20of%20LML-type%20structured%20lipids.pdf |
| _version_ | 1796980733723541504 |
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| author | Lian, Weishuai Wang, Weifei Tan, Chin Ping Wang, Jianrong Wang, Yonghua |
| author_facet | Lian, Weishuai Wang, Weifei Tan, Chin Ping Wang, Jianrong Wang, Yonghua |
| author_sort | Lian, Weishuai |
| collection | UPM |
| description | LML-type structured lipids are one type of medium- and long-chain triacylglycerols. LML was synthesized using immobilized Talaromyces thermophilus lipase (TTL)-catalyzed interesterification of tricaprylin and ethyl linoleate. The resin AB-8 was chosen, and the lipase/support ratio was determined to be 60 mg/g. Subsequently, the immobilized TTL with strict sn-1,3 regiospecificity was applied to synthesize LML. Under the optimized conditions (60 °C, reaction time 6 h, enzyme loading of 6% of the total weight of substrates, substrate of molar ratio of ethyl linoleate to tricaprylin of 6:1), Triacylglycerols with two long- and one medium-chain FAs (DL-TAG) content as high as 52.86 mol% was obtained. Scale-up reaction further verified the industrial potential of the established process. The final product contained 85.24 mol% DL-TAG of which 97 mol% was LML after purification. The final product obtained with the high LML content would have substantial potential to be used as functional oils. |
| first_indexed | 2024-03-06T10:27:24Z |
| format | Article |
| id | upm.eprints-80148 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T10:27:24Z |
| publishDate | 2019 |
| publisher | Springer |
| record_format | dspace |
| spelling | upm.eprints-801482020-09-30T08:24:39Z http://psasir.upm.edu.my/id/eprint/80148/ Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids Lian, Weishuai Wang, Weifei Tan, Chin Ping Wang, Jianrong Wang, Yonghua LML-type structured lipids are one type of medium- and long-chain triacylglycerols. LML was synthesized using immobilized Talaromyces thermophilus lipase (TTL)-catalyzed interesterification of tricaprylin and ethyl linoleate. The resin AB-8 was chosen, and the lipase/support ratio was determined to be 60 mg/g. Subsequently, the immobilized TTL with strict sn-1,3 regiospecificity was applied to synthesize LML. Under the optimized conditions (60 °C, reaction time 6 h, enzyme loading of 6% of the total weight of substrates, substrate of molar ratio of ethyl linoleate to tricaprylin of 6:1), Triacylglycerols with two long- and one medium-chain FAs (DL-TAG) content as high as 52.86 mol% was obtained. Scale-up reaction further verified the industrial potential of the established process. The final product contained 85.24 mol% DL-TAG of which 97 mol% was LML after purification. The final product obtained with the high LML content would have substantial potential to be used as functional oils. Springer 2019 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/80148/1/Immobilized%20Talaromyces%20thermophilus%20lipase%20as%20an%20efficient%20catalyst%20for%20the%20production%20of%20LML-type%20structured%20lipids.pdf Lian, Weishuai and Wang, Weifei and Tan, Chin Ping and Wang, Jianrong and Wang, Yonghua (2019) Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids. Bioprocess and Biosystems Engineering, 42 (2). pp. 321-329. ISSN 1615-7591; ESSN: 1615-7605 https://www.researchgate.net/publication/328895530_Immobilized_Talaromyces_thermophilus_lipase_as_an_efficient_catalyst_for_the_production_of_LML-type_structured_lipids 10.1007/s00449-018-2036-7 |
| spellingShingle | Lian, Weishuai Wang, Weifei Tan, Chin Ping Wang, Jianrong Wang, Yonghua Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids |
| title | Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids |
| title_full | Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids |
| title_fullStr | Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids |
| title_full_unstemmed | Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids |
| title_short | Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids |
| title_sort | immobilized talaromyces thermophilus lipase as an efficient catalyst for the production of lml type structured lipids |
| url | http://psasir.upm.edu.my/id/eprint/80148/1/Immobilized%20Talaromyces%20thermophilus%20lipase%20as%20an%20efficient%20catalyst%20for%20the%20production%20of%20LML-type%20structured%20lipids.pdf |
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