Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids
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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.
KeywordsTalaromyces thermophilus lipase Immobilization Interesterification Structured lipids Functional oils
Talaromyces thermophilus lipase
This work was supported by the National Outstanding Youth Science Foundation of China (31725022), Molecular Enzyme and Engineering International Cooperation Base of South China University of Technology (2017A050503001), Special Program of Guangdong Province for Leader Project in Science and Technology Innovation: Development of New Partial Glycerin Lipase (2015TX01N207), and Science and Technology Planning project of Guangdong province (2016B090920082).
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Conflict of interest
The authors have declared no conflict of interest.
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