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Characterization of polyphenol oxidase activity in a range of forage ecotypes with different phenol substrates. A new insight for PPO and protein‐bound phenol evaluation
Authors:A. Cabiddu  M. R. F. Lee  M. Decandia  G. Molle  L. Salis  M. Vargiu  A. L. Winters
Affiliation:1. Dipartimento per la Ricerca nelle Produzioni Animali, Agris, , Olmedo, Italy;2. School of Veterinary Sciences, University of Bristol, , Langford, UK;3. Dipartimento per la Ricerca nelle Produzioni Vegetali, Agris, , Cagliari, Italy;4. Institute of Biological, Environmental and Rural Sciences, Aberystwyth University, , Aberystwyth, UK
Abstract:Plant phenols can influence utilization of forages by ruminants through binding with proteins either by complexing with oxidized phenols (products of polyphenol oxidase activity or formed in oxidizing conditions) or by hydrogen binding with tannins. These protein‐bound phenols (PBPs) affect rumen metabolism by inhibition of both proteolysis and lipolysis. The aim of this work was to assess the level of polyphenol oxidase (PPO) activity (determined with a range of diphenolic substrates), PBP content, and to identify the main source of variation in different forage ecotypes harvested at different phenological stages. PPO activity was strongly influenced by substrate type with a significant effect of forage ecotype. Forage ecotype and phenological stage also influenced PPO and PBP content. PPO showed a strong relationship with dry matter and phenol content of plants.
Keywords:polyphenol oxidase  forage ecotype  plant secondary metabolites  protein‐bound phenol
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