Abstract
Bovine serum albumin (BSA) and BSA-glucose conjugates (GBSAⅠ and GBSAⅠI) with different extent of glycation were complexed with curcumin (CUR). The formation mechanism of BSA/GBSA-CUR complexes and the effect of glycation on their physicochemical properties were investigated. Fluorescence quenching and FTIR analysis indicated that the BSA/GBSA–CUR nanocomplexes were formed mainly by hydrophobic interactions. XRD analysis demonstrated that CUR was present in an amorphous state in the nanocomplexes. BSA with a greater extent of glycation (BSA < GBSAⅠ<GBSAⅠI) displayed a higher binding affinity for CUR. The highest CUR encapsulation efficiency (86.77%) and loading capacity (7.81 mg/g) were obtained in the GBSAⅠI-CUR nanocomplex. The zeta-potential varied from −17.45 to −27.65 mV, depending on the extent of glycation. Furthermore, the physicochemical stability of BSA/GBSA-CUR nanocomplexes increased with the increasing extent of glycation of BSA. Thus, the obtained GBSAⅠI have the potential to become new delivery carriers for encapsulating hydrophobic food components.
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