Abstract
The optimum conditions for decolorization of an azo dye, C.I. Reactive Black 5 (RB5) and the kinetic characteristics of manganese-dependent peroxidase (MnP) production by yeast isolate, Debaryomyces polymorphus, were investigated. D. polymorphus could completely degrade 200 mg l −1 of non-hydrolyzed and hydrolyzed C.I. Reactive Black 5 within 24 h of cultivation at an inoculum size of 1.4 g l −1 wet cells in 50 ml medium consisting of 5 g l −1 glucose and 0.5–1.0 g l −1 ammonium sulphate (pH 5–7). In addition, the MnP activities during the cultivation were evaluated in the absence and presence of 200 mg l −1 C.I. Reactive Black 5. Maximum activity of MnP (1555.6 U l −1) was detected at 24 h cultivation in the presence of the dye, and a significant reduction of the enzyme activity was observed thereafter. The presence of C.I. Reactive Black 5 in the culture was found to be indispensable to the production of MnP by D. polymorphus. A good correlation was found between the dye degradation and the enzyme production.
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