Rationale behind the near-ideal catalysis of Candida antarctica lipase A (CAL-A) for highly concentrating ω-3 polyunsaturated fatty acids into monoacylglycerols

Abstract

Dramatic decline in the quality and quantity of ω-3 PUFAs from marine resource demands new environmental-friendly technology to produce high quality ω-3 PUFAs concentrates in a better bioavailable form. Accordingly this work demonstrated an exceptionally highly efficient non-aqueous approach that non-regiospecific and non ω-3 PUFAs preferential Candida antarctica lipase A (CAL-A), functioning as a near-ideal biocatalyst, is capable to directly concentrate ω-3 PUFAs from 20% to 30% in oils to up to >90% in monoacylglycerols form through one step reaction. The rationale behind the experimental observation is justified and the catalytic property and specificity of an ideal enzyme tackling this task are defined. High selectivity and efficiency, excellent reusability of biocatalyst, general applicability for concentrating ω-3 PUFAs from both fish and microalgae oils, simple process for product recovery (e.g. by short path distillation), make this novel approach a highly industrially relevant and with potential application in food and drug industries.

Keywords: Candida antarctica lipase A (CAL-A); Docosahexaenoic acid (PubChem CID: 445580); Eicosapentaenoic acid (PubChem CID: 446284); Ethanol (PubChem CID: 702); Ethanolysis; Fish oil; Monoacylglcerols (MAGs); Oleic acid (PubChem CID: 445639); Palmitic acid (PubChem CID: 985); Stearidonic acid (PubChem CID: 5312508); α-Linolenic acid (PubChem CID: 5280934); ω-3 Polyunsaturated fatty acids (ω-3 PUFAs).