To clarify the role of pear peroxidase (POD) in enzymatic browning, oxidation of 4-methylcatechol, chlorogenic acid, and (−)-epicatechin catalyzed by purified polyphenol oxidase (PPO), purified POD, or combinations of the two enzymes was followed by HPLC. It was shown that pear POD had no oxidative (oxygen dependent) activity. However, in presence of PPO, POD enhanced the phenol degradation. Moreover, when PPO was entirely inhibited by NaCl after different oxidation times, addition of POD led to a further consumption of the phenolic compound. Two mechanisms have been proposed to explain this additional consumption. First, our results have demonstrated that, whatever the substrate used, PPO oxidation generated H2O2, the amount of which varies with the phenolic structure. Second, quinonic forms are used by POD as peroxide substrate. These two mechanisms associated with the kinetic properties of pear PPO and POD are consistent with an effective involvement of pear POD in enzymatic browning. Keywords: Enzymatic browning; pear; peroxidase; polyphenol oxidase

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The greater ability of some strains to germinate in response to l-alanine and inosine is one criterion among others for B. cereus strain selection in food processing or storage studies, before confirmation in complex food or laboratory media. The diversity in response to germinants found among the B. cereus strains suggests a differential expression and (or) absence of some germination genes involved in the response, mainly to l-alanine.