Encapsulation of lipases on coordination polymers and their catalytic performance in glycerolysis and esterification

Abstract

In this study, lipases of CALB (Candida antarctica lipase B), TLL (Thermomyces lanuginosa lipase), RML (Rhizomucor miehei lipase), CALA (Candida antarctica lipase A) and LU (Lecitase® Ultra) were encapsulated into the nucleotide-hybrid metal coordination polymers (CPs) for diacylglyerols (DAG) preparation. Guanosine 5′-monophosphate (GMP) and adenosine 5′-monophosphate (AMP) were used as coordinating molecules, and metal ions of Fe3+, Ba2+, Mn2+, Ni2+ and Cr3+ were applied to prepare matrix. Results indicated that, besides Ba2+ with AMP, all other metal ions can coordinate with AMP and GMP to generate CPs. In addition, the AMP/Ni was amorphous when standing temperature was 4 °C, while it was crystalline when standing temperature was from 30 to 180 °C. DAG content from 47.55% to 64.99% was obtained from glycerolysis by CALB@GMP/Ba, RML@GMP/Ba, TLL@GMP/Ba, RML@GMP/Mn and TLL@GMP/Mn. Additionally, CALB@GMP/Fe showed selectivity towards DAG formation in the esterification and DAG content up to 61.88% was obtained.

Keywords

• Lipase
• Coordination polymers
• Encapsulation
• Glycerolysis
• Esterification