Synthesis and characterization of enzymatically cross-linked feruloyl amylopectin for curcumin encapsulation

Feruloyl amylopectin (FAP) was synthesized by the N,N'-carbonyldiimidazole (CDI) activation method, and the enzymatically cross-linked feruloyl amylopectin (CL-FAP) was prepared via catalysis of horseradish peroxidase (HRP) with the presence of hydrogen peroxide (H2O2). RP-HPLC-DAD/ESI-TOF-MS measured ferulic acid and its derivatives in FAP and CL-FAP. FAP was primarily composed of two ferulate monomers, while CL-FAP was composed of two ferulate monomers and two ferulate dehydrodimers. The ester formation in the feruloyl group was confirmed by the presence of carbonyl and aromatic C=C signal near 1725 (1723) and 1510 cm(-1) in the FT-IR spectra. X-ray diffraction studies showed that the two modified amylopectins lost the ordered A-type crystalline structure, characteristic of maize amylopectin. The encapsulation capacity of curcumin (ECC) in 1 mg/mL CL-FAP microemulsion was measured at 88.13 mu g/mg by HPLC. (C) 2015 Elsevier B.V. All rights reserved.