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

- Rationale for enzymatic concentration of n-3 PUFAs into glycerides is defined.
- Non-regiospecificity & high non-n-3 PUFAs preference are ideal catalytic feature.
- CAL-A identified as a near-ideal enzyme for concentrating n-3 PUFAs via ethanolysis.
- CAL-A affords concentration efficacy of n-3 PUFAs from 25% in oil to 90% in MAGs.
- 13CNMR analysis verifies the conceptual hypothesis and reveals catalytic mechanism.

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.

Non-regiospecific and non ω-3 PUFAs preferential catalytic specificities enable Candida antarctica lipase A (CAL-A), to function as a near-ideal biocatalyst, and concentrate ω-3 PUFAs from 20% to 30% in oils to up to >90% (close to a theoretical value) in monoacylglycerols (MAGs) through one step ethanolysis.