Polyphenolic substrates of cationic and neutral/anionic peroxidases from barley and malt using a chronometric method for the determination of pod activity

4-methylcatechol, phenolic acids from the benzoic and cinnamic series, flavan 3-ols and L-tyrosine were tested to determine the catalytic behavior of barley peroxidases (POD) at the expense of hydrogen peroxide. A chronometric assay using L-ascorbic acid was described for determining the peroxidatic activity of basic and neutral/anionic enzymatic fractions. The effects of hydrogen donors H2O2, and Ca++ ion concentrations and pH were studied to set maximal conditions for POD measurement. The sensitivity to endogenous phenolic compounds (ferulic and p-coumaric acids, (+) catechin) along with caffeic acid for POD fractions was investigated and compared with their response versus guaiacol. Under the conditions tested, syringic and sinapinic acids as well as L-tyrosine were very weakly oxidized by POD from barley, whereas ferulic and caffeic acids were rapidly transformed. Levels of POD activity extracted from barley, green malt and kilned malt crude extracts were thereafter compared.