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...
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Main Authors: | , , , , |
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Format: | Article |
Language: | English |
Published: |
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 http://psasir.upm.edu.my/id/eprint/80148/ https://www.researchgate.net/publication/328895530_Immobilized_Talaromyces_thermophilus_lipase_as_an_efficient_catalyst_for_the_production_of_LML-type_structured_lipids |
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Summary: | 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. |
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