Synthesis of conjugated linoleic acid-rich triacylglycerols by immobilized mutant lipase with excellent capability and recyclability

Lian W 1 , Li D 1 , Zhang L 2 , Wang W 3 , Faiza M 1 , Tan CP 4 Show all authors , Yang B 5 , Lan D 6 , Wang Y 7

Affiliations 

  • 1 School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China
  • 2 College of Life Science, Tarim University, Alar 843300, China
  • 3 Sericultural and Agri-food Research Institute, Guangdong Academy of Agricultural Sciences, Guangzhou 510610, China
  • 4 Department of Food Technology, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400, UPM Serdang, Selangor, Malaysia
  • 5 School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China
  • 6 School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China. Electronic address: [email protected]
  • 7 School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China; Guangdong Research Center of Lipid Science and Applied Engineering Technology, South China University of Technology, Guangzhou 510640, China. Electronic address: [email protected]
Enzyme Microb Technol, 2018 Oct;117:56-63.
PMID: 30037552 DOI: 10.1016/j.enzmictec.2018.06.007

Abstract

Conjugated linoleic acid (CLA)-rich triacylglycerols (TAG) have received significant attention owing to their health promoting properties. In this study, CLA-rich TAG were successfully synthesized by an immobilized mutant lipase (MAS1-H108A)-catalyzed esterification of CLA-rich fatty acids and glycerol under vacuum. MAS1-H108A was first immobilized onto ECR1030 resin. Results showed that the lipase/support ratio of 41 mg/g was suitable for the immobilization and the thermostability of immobilized MAS1-H108A was greatly enhanced. Subsequently, the immobilized MAS1-H108A was employed for the synthesis of CLA-rich TAG and 95.21% TAG with 69.19% CLA was obtained under the optimized conditions. The TAG content (95.21%) obtained by immobilized MAS1-H108A is the reported highest value thus far, which was significantly higher than that (9.26%) obtained by Novozym 435 under the same conditions. Although the TAG content comparable to the results obtained in this study could also be obtained by Novozym 435, the used enzyme amount is approximately 5-fold of the immobilized MAS1-H108A. Additionally, the immobilized MAS1-H108A exhibited excellent recyclability during esterification retaining 95.11% of its initial activity after 10 batches. Overall, such immobilized mutant lipase with superior esterification activity and recyclability has the potential to be used in oils and fats industry.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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