Nanocomplexes of curcumin and glycated bovine serum albumin: The formation mechanism and effect of glycation on their physicochemical properties. (30th January 2022)

• Record Type: Journal Article
• Authors: Fu, Jing-jing; Sun, Cong; Tan, Zhi-feng; Zhang, Guang-yao; Chen, Gui-bing; Song, Liang
• Is Part Of: Food chemistry. Volume 368(2022)
• Publication Date: 2022-01-30
• Subjects: Bovine serum protein; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2021.130651
• Languages: English
• ISSNs: 0308-8146

Abstract

Graphical abstract: Highlights: BSA and BSA-glucose conjugates (GBSA) complexed with curcumin (CUR) were fabricated. The interaction of CUR and BSA or GBSA was spontaneous. BSA/GBSA–CUR nanocomplexes were formed mainly by hydrophobic interactions. Increasing the extent of glycation promoted physicochemical stability of nanocomplexes. 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.