Oxidative phenols in forage crops containing polyphenol oxidase enzymes.
Polyphenol oxidases (PPOs) are copper-containing enzymes that catalyze oxidation of endogenous monophenols to ortho-dihydroxyaryl compounds and of ortho-dihydroxyaryl compounds to ortho-quinones. Subsequent nucleophilic addition reactions of phenols, amino acids, and proteins with the electrophilic ortho-quinones form brown-, black-, or red-colored secondary products associated with the undesired discolouration of fruit and vegetables. Several important forage plants also exhibit significant PPO activity, and a link with improved efficiency of ruminant production has been established. In ruminant animals, extensive degradation of forage proteins, following consumption, can result in high rates of excretion of nitrogen, which contributes to point-source and diffuse pollution. Reaction of quinones with forage proteins leads to the formation of protein-phenol complexes that are resistant to proteolytic activity during ensilage and during rumen fermentation. Thus, PPO in red clover (Trifolium pratense) has been shown to improve protein utilization by ruminants. While PPO activity has been demonstrated in a number of forage crops, little work has been carried out to identify substrates of PPO, knowledge of which would be beneficial for characterizing this trait in these forages. In general, a wide range of 1,2-dihydroxyarenes can serve as PPO substrates because these are readily oxidized because of the ortho positioning of the hydroxy groups. Naturally occurring phenols isolated from forage crops with PPO activity are reviewed. A large number of phenols, which may be directly or indirectly oxidized as a consequence of PPO activity, have been identified in several forage grass, legume, cereal, and brassica species; these include hydroxybenzoic acids, hydroxycinnamates, and flavonoids. In conclusion, a number of compounds are known or postulated to enable PPO activity in important PPO-expressing forage crops. Targeting the matching of these compounds with PPO activity would be a useful plant breeding approach to improve the utilization of feed nitrogen by ruminant livestock and help reduce the environmental impact of livestock agriculture in temperate countries.
Parveen
Ifat
I
Institute of Biological, Environmental and Rural Sciences, Aberystwyth University, Gogerddan, Aberystwyth SY23 3EB, UK. ifp@aber.ac.uk
Threadgill
Michael D
MD
Moorby
Jon M
JM
Winters
Ana
A
D000821:Animal Feed / Q000032:analysis; D000818:Animals; D000829:Animals, Domestic / Q000378:metabolism; D004156:Catechol Oxidase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism
D010636:Phenols; D010940:Plant Proteins; D004156:Catechol Oxidase