The aim of this study was to investigate the biochemical properties of free and immobilized mushroom tyrosinase (EC 1.14.18.1) entrapped in calcium alginate beads for phenol oxidation in a batch system. Tyrosinase activity was determined spectrophotometrically at 400 nm under optimal conditions. The effects of key operational parameters on phenol oxidation kinetics were evaluated for both enzyme systems. The Michaelis–Menten constant (KM) of the immobilized enzyme (0.94 ± 0.2 mM) was approximately twice that of the free enzyme (0.56 ± 0.04 mM), while its maximum reaction velocity (VMax = 101.4 ± 2.2 µmol L−1 min−1) decreased by nearly 30-fold (VMax(App) = 3.63 ± 0.3 µmol L−1 min−1). Immobilization also shifted the optimal pH of the enzyme to pH 6.0. The optimum temperature and activation energy for phenol oxidation were determined as 55 °C and 52.48 kJ/mol for immobilized tyrosinase, whereas they were 45 °C and 39.58 kJ/mol for the free enzyme. The highest level of activity was obtained with alginate beads of 2.6 mm diameter, and the immobilized preparation exhibited enhanced operational stability, completely retaining its initial activity after five reuse cycles. Overall, these findings suggest that mushroom tyrosinase immobilized in alginate beads is a promising system for phenol removal from wastewater.
Leboukh et al. (Tue,) studied this question.
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