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Immobilized Talaromyces thermophilus lipase as an efficient catalyst for the production of LML-type structured lipids


Citation

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

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.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Food Science and Technology
DOI Number: https://doi.org/10.1007/s00449-018-2036-7
Publisher: Springer
Keywords: Talaromyces thermophilus lipase; Immobilization; Interesterification; Structured lipids; Functional oils
Depositing User: Azhar Abdul Rahman
Date Deposited: 30 Sep 2020 07:36
Last Modified: 30 Sep 2020 08:24
Altmetrics: http://altmetrics.com-details.php?domain=psair.upm.edu.my&doi= 10.1007/s00449-018-2036-7
URI: http://psasir.upm.edu.my/id/eprint/80148
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