Impact of covalent or non-covalent bound epigallocatechin-3-gallate (EGCG) on assembly, physicochemical characteristics and digestion of ovotransferrin fibrils

Zihao Wei, Qingrong Huang

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

The objectives of the present study were to investigate impact of covalent or non-covalent bound (−)-epigallocatechin-3-gallate (EGCG) on ovotransferrin (OVT) fibrils. Bound EGCG showed fibril-inhibitory activity in a concentration-dependent manner, and covalent bound EGCG inhibited OVT fibrillation more intensely than an equal amount of non-covalent bound EGCG. Bound EGCG resulted in larger fibril building blocks. Covalent bound EGCG shortened OVT fibrils significantly, and non-covalent bound EGCG induced smaller changes in length of OVT fibrils than covalent bound EGCG. A larger amount of covalent or non-covalent bound EGCG led to shorter OVT fibrils. Covalent bound EGCG did not change thickness of OVT fibrils, while newly emerged thicker fibrils were observed in the presence of non-covalent bound EGCG. Covalent bound EGCG shifted isoelectric point of OVT fibril to lower pHs than non-covalent bound EGCG. Bound EGCG decreased surface hydrophobicity, storage modulus and viscosity of OVT fibrils. OVT fibrils with bound EGCG possessed strong antioxidant capacity. The gastrointestinal digestion result demonstrated that covalent bound EGCG contributed to a higher increase in fibril digestibility than non-covalent bound EGCG.

Original languageEnglish (US)
Article number105314
JournalFood Hydrocolloids
Volume98
DOIs
StatePublished - Jan 2020

All Science Journal Classification (ASJC) codes

  • Food Science
  • Chemistry(all)
  • Chemical Engineering(all)

Keywords

  • (−)-Epigallocatechin-3-gallate
  • Covalent binding
  • In vitro digestibility
  • Non-covalent binding
  • Ovotransferrin fibril
  • Rheology

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