Related Experiment Video
Updated: Feb 2, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids
Weishuai Lian1, Weifei Wang2, Chin Ping Tan3
1School of Food Science and Engineering, South China University of Technology, Guangzhou, 510640, China.
Abstract:
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.
Related Concept Videos
Structure of Lipids
Structure of Lipids
Lipid Digestion
Production Efficiency
Structural Steel Products
Once shaped, the steel's final form emerges as a continuous length, which is then segmented by a hot saw into manageable pieces. These segments...
What are Lipids?

