Enhanced catalysis of Yarrowia lipolytica lipase LIP2 immobilized on macroporous resin and its application in enrichment of polyunsaturated fatty acids.
An immobilization strategy was employed to improve activity and operational stability of Yarrowia lipolytica lipase LIP2 (YlLIP2) by using macroporous resins as carrier. D152H, a cation-exchange resin, was the best support. Under the optimized conditions, the immobilization efficiency was 89.81% and the specific activity was 809,751 U/g, being 2.1-fold higher than that of the free lipase. Bioimprinting and interfacial activation were used to further boost the catalytic activity of YlLIP2, respectively enhanced 21.5-fold, 231.2% and 107.2% compared to the free, non-bioimprinted and non-interfacial-activated lipases. The immobilized lipase exhibited much better thermal and pH stability and broader substrate specificity; when used to enrich docosahexaenoic acid (DHA) from Chlorella protothecoides oil, it could increase 1.66-fold of DHA content and show good operational stability. These indicate that the immobilized YlLIP2 offers a promising approach for the enrichment of DHA.
Key Laboratory of Molecular Biophysics, The Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China. yanyunjun@mail.hust.edu.cn
Yunjun
Y
Yan
Xiaoyan
X
Zhang
Dawei
D
Chen
D000327:Adsorption; D002384:Catalysis; D002411:Cation Exchange Resins / Q000737:chemistry*; D004281:Docosahexaenoic Acids / Q000138:chemical synthesis*; D004789:Enzyme Activation; D004800:Enzymes, Immobilized / Q000737:chemistry; D005231:Fatty Acids, Unsaturated / Q000138:chemical synthesis; D005656:Fungal Proteins / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry*; D010938:Plant Oils / Q000737:chemistry*; D016062:Porosity
D002411:Cation Exchange Resins; D004800:Enzymes, Immobilized; D005231:Fatty Acids, Unsaturated; D005656:Fungal Proteins; D010938:Plant Oils; D004281:Docosahexaenoic Acids; C408971:LIP2 protein, Yarrowia lipolytica; D008049:Lipase