Characterization of tyrosinase- and polyphenol esterase-catalyzed end products using selected phenolic substrates.
The oxidative end products that result from the biocatalysis of tyrosinase (PPO) and/or a polyphenol esterase (PPE) extract have been investigated simultaneously in model systems containing selected phenolic compounds as substrates. The spectrophotometric scanning of brown color, formed in the presence of both PPO and PPE, showed a decrease in the absorbance compared to that obtained with PPO only. Graphical analyses of the iterative spectra of oxidized phenolic end products by PPO confirmed the presence of, at least, three kinetically related absorbing species. HPLC analyses of the end products, obtained by the biocatalysis of PPE or PPO activity, indicated the presence of two main groups of compounds: colored ones of lambda(max) at 294-324 nm and colorless products of lambda(max) at 264-290 nm. PPE produced both compounds when selected substrates were used as substrates, whereas PPO produced only one type of oxidation product. However, when both enzymes were incubated together, the nature of the end products was similar to that obtained with PPE only.
Madani
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W
Department of Food Science and Agricultural Chemistry, McGill University, Quebec, Canada.
Kermasha
S
S
Versari
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D000363:Agaricales / Q000201:enzymology; D001234:Aspergillus niger / Q000201:enzymology; D004950:Esterases / Q000378:metabolism*; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D010636:Phenols / Q000378:metabolism*; D013379:Substrate Specificity
D010636:Phenols; D014442:Monophenol Monooxygenase; D004950:Esterases