Synthesis of lipase/silica biocatalysts through the immobilization of CALB on porous SBA-15 and their application on the resolution of pharmaceutical derivatives and on nutraceutical enrichment of natural oil

Abstract

• A recombinant lipase was produced in a low-cost medium. • The immobilization process was studied. • The use of ammonium fluoride, APTES and GA allowed a most active biocatalyst. • Resolution of racemic myo -inositol derivatives was done with eep>99 %. • It was possible to obtain lipids containing 181.6 mg of EPA and DHA in coconut oil. A recombinant lipase from Candida antarctica , LIPB, was obtained through fermentation using an alternative low-cost medium and immobilized on the distinct mesoporous silica particles. The performance and versatility of the new biocatalysts was evaluated, for the first time, on two biotechnological interest reactions: resolution of racemic myo-inositol derivative and acidolysis reaction of coconut oil. For the racemate, the covalent biocatalyst SBA-15-F-APTES-GA-LIPB exhibited the highest conversions and enantiomeric excess of up to 99 %. It was the first time that covalent biocatalyst was used for resolution of racemic myo-inositol derivative. The most active biocatalyst (SBA-15-F-APTES-GA-LIPB) was used on ten different reaction cycles maintaining its activity, highlighting the operational stability of the developed biocatalyst. Moreover, it was possible to produce food oils enriched with polyunsaturated fatty acids (PUFA), obtaining lipids containing 181.6 mg of EPA and DHA in coconut oil. The preliminary economic analyses also indicate that the enzymatic production of such nutraceuticals and pharmaceutics compounds may be economically feasible, principally exploring low-cost strategies for enzyme production.