Polyphenol-protein complexes and their consequences for the redox activity, structure and function of honey. A current view and new hypothesis - a review

• Autorzy: Brudzynski K. , Maldonado-Alvarez L.
• Języki publikacji: EN

Abstrakty

EN

There is increasing evidence that protein complexation by honey polyphenols is changing honey structure and function. This relatively less investigated filed of honey research is presented in a context of known mechanism of formation of the stable polyphenol-protein complexes in other foods. At a core of these interactions lies the ability of polyphenols to form non-covalent and covalent bonds with proteins leading to transient and/or irreversible complexes, respectively. Honey storage and thermal processing induces non-enzymatic oxidation of polyphenols to reactive quinones and enables them to form covalent bonds with proteins. In this short review, we present data from our laboratory on previously unrecognized types of protein-polyphenol complexes that differed in size, stoichiometry, and antioxidant capacities, and the implications they have to honey antioxidant and antibacterial activities. Our intent is to provide a current understanding of protein-polyphenol complexation in honey and also some new thoughts /hypotheses that can be useful in directing future research.

Słowa kluczowe

EN

polyphenol-protein complex; polyphenol-protein interaction; consequence; redox activity; structure; function; honey; new hypothesis; hypothesis; quinone

• Wydawca: -
• Czasopismo: Polish Journal of Food and Nutrition Sciences
• Rocznik: 2015
• Tom: 65
• Numer: 2
• Opis fizyczny: p.71-80,fig.,ref.

Twórcy

autor

Brudzynski K.

• Department of Drug Discovery and Development, Bee-Biomedicals Inc., A9–210 Glendale Ave., Suite 109, St.Catharines, ON, L2T 3Y6, Ontario, Canada

autor

Maldonado-Alvarez L.

• Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada

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Identyfikatory

DOI

10.1515/pjfns-2015-0030