Abstract o‐Diphenolase extracted from Triticum aestivum (cv. Nettuno) and purified in various steps gave a 250‐fold purification over the crude extract. This purified enzyme showed maximum relative activity towards 4‐methylcatechol, generally high or moderate activity towards di‐ and polyphenols, and very low activity towards monophenols. Total activity, determined at each step of purification, showed that treatment with ammonium sulphate and calcium phosphate gel gave rise to an activation of o‐diphenolase, thus revealing a latency of enzymatic activity. In the pH profile activity towards 4‐methylcatechol two optima at pH 5.3 and 6.9 were observed.
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Interesse et al. (1980) studied this question.
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