4.7 Article

Improved curcumin bioaccessibility in Pickering emulsion fabricated by rice glutelin fibrils

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FOOD BIOSCIENCE
卷 55, 期 -, 页码 -

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ELSEVIER
DOI: 10.1016/j.fbio.2023.102988

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Rice glutelin fibrils; Pickering emulsion; Curcumin bioavailability

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This study successfully fabricated rice glutelin fibrils-stabilized Pickering emulsion for loading curcumin. It was found that the fibril-stabilized emulsion showed high curcumin encapsulation efficiency and strong gel strength, while the particle-prepared emulsion exhibited weak gel strength and rapid curcumin release. Overall, the sustainable and biocompatible protein amyloid showed excellent performance in encapsulating curcumin and improving curcumin bioavailability.
Pickering emulsion fabricated by food grade-solid colloidal particles as templates for delivering sensitive nutrients has attracted increasing interest in recent years. In this work, rice glutelin fibrils-stabilized Pickering emulsion was successfully fabricated for loading curcumin. In addition, the amyloid and non-amyloid structures were separated from the heated rice glutelin (RG) samples, and the emulsifying and encapsulating performances of these fractions were systematically observed. It was noted that the retentates of glutelin fibrils (RGFs)-stabilized Pickering emulsion exhibited a self-standing behavior, along with the highest curcumin encapsulation efficiency (94.17%) among other samples. Compared to the total heated glutelin fibrils (TGFs), a stronger gel strength was observed in emulsion containing purified fibrils, probably due to the closely arranged polyhedral emulsion structure. However, the filtrates of glutelin fibrils (FGFs) particles-prepared emulsion presented a weak gel strength due to the hydrophilic properties, accompanying by a surprisingly rapid release rate of curcumin during digestion. Nevertheless, TGFs-stabilized emulsion achieved a high curcumin bioavailability (35.06%) and sustained controlled release behavior. These findings proved that the sustainable and biocompatible protein amyloid exhibited excellent performance in encapsulating curcumin and improving curcumin bioavailability.

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