Insight of Stability of Procyanidins in Free and Liposomal Form under an in Vitro Digestion Model: Study of Bioaccessibility, Kinetic Release Profile, Degradation, and Antioxidant Activity

J Agric Food Chem. 2019 Feb 20;67(7):1990-2003. doi: 10.1021/acs.jafc.9b00351. Epub 2019 Feb 8.

Abstract

Small unilamellar and multilayered liposomes loaded with polymeric (epi)catechins up to pentamers were produced. The bioaccessibility, kinetic release profile, and degradation under in vitro gastrointestinal conditions were monitored by UHPLC-DAD-QTOF-MS/MS. The results show that all of the procyanidins underwent depolymerization and epimerization into small molecular oligomers and mainly to (epi)catechin subunits. Moreover, all of the liposome formulations presented higher bioaccessibility and antioxidant activity in comparison to their respective counterparts in non-encapsulated form. Similar results were obtained with procyanidins from cocoa extract-loaded liposomes. Namely, the bioaccessibility of dimer, trimer, and tetramer fractions from cocoa-loaded liposomes were 4.5-, 2.1-, and 9.3-fold higher than those from the non-encapsulated cocoa extract. Overall, the procyanidin release profile was dependent on their chemical structure and physicochemical interaction with the lipid carrier. These results confirmed that liposomes are efficient carriers to stabilize and transport procyanidins with the aim of enhancing their bioaccessibility at a controlled release rate.

Keywords: bioaccessibility; cocoa procyanidins; in vitro digestion; liposomes.

MeSH terms

  • Antioxidants / metabolism*
  • Biological Availability
  • Calcium-Binding Proteins / chemistry
  • Catechin / metabolism
  • Chemical Phenomena
  • Digestion
  • Drug Stability
  • Kinetics
  • Liposomes* / chemistry
  • Liposomes* / metabolism
  • Microscopy, Electron, Transmission
  • Molecular Structure
  • Pancreatin / metabolism
  • Pepsin A / metabolism
  • Proanthocyanidins / chemistry
  • Proanthocyanidins / metabolism*
  • Proanthocyanidins / pharmacokinetics*
  • Transcription Factors

Substances

  • Antioxidants
  • Calcium-Binding Proteins
  • Calcoco1 protein, mouse
  • Liposomes
  • Proanthocyanidins
  • Transcription Factors
  • Pancreatin
  • Catechin
  • Pepsin A