Non-covalent binding of chlorogenic acid to myofibrillar protein improved its bio-functionality properties and metabolic fate

Zhiwei Zhou, Dan Wang, Dongmei Luo, Zhiqiang Zhou, Wei Liu, Weicai Zeng, András Dinnyés, Youling L. Xiong, Qun Sun

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

As natural antioxidants added to meat products, polyphenols can interact with proteins, and the acid-base environment influenced the extent of non-covalent and covalent interactions between them. This study compared the bio-functional characteristics and metabolic outcomes of the myofibrillar protein-chlorogenic acid (MP-CGA) complexes binding in different environments (pH 6.0 and 8.5). The results showed that CGA bound with MP significantly enhanced its antioxidant activity and inhibitory effect on metabolism enzymes. CGA bound deeply into the MP structure hydrophobic cavity at pH 6.0, which reduced its degradation by digestive enzymes, thus increasing its bio-accessibility from 59.5% to 71.6%. The digestion products of the two complexes exhibited significant differences, with the non-covalent MP-CGA complexes formed at pH 6.0 showing significantly higher concentrations of rhetsinine and piplartine, two well-known compounds to modulate diabetes. This study demonstrated that non-covalent binding between protein and polyphenol in the acidic environment held greater promising prospects for improving health.

Original languageEnglish
Article number138208
JournalFood Chemistry
Volume440
DOIs
StatePublished - May 15 2024

Bibliographical note

Publisher Copyright:
© 2023 Elsevier Ltd

Keywords

  • Bio-functional properties
  • Chlorogenic acid
  • Metabolic fate
  • Non-covalent binding
  • Polyphenol bio-accessibility

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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