Enzymatic decolorization of melanoidins from molasses wastewater by immobilized keratinase.

The aim of this work was to study the ability of commercial immobilized hydrolases in the decolorization of molasses wastewater. Commercial immobilized keratinase obtained the highest decolorization yield (86.6-91.1%) among all of commercial immobilized enzymes tested. Immobilized keratinase had the potential to replace immobilized oxidoreductase to decolorize molasses wastewater. Keratinase from Meiothermus taiwanensis WR-220 (KMT) immobilized on modified bagasse cellulose obtained a decolorization yield of 84.7-90.2%. It removed 60.2-65.6% of colorants and 61.4-69.8% of chemical oxygen demand (COD) for 5 days continuously. Notably, the treatment cost was less than 0.15 dollar per ton. Immobilized KMT-wt had similar performance with commercial immobilized keratinase in bleaching molasses wastewater. Importantly, it was more economic. Finally, the results confirmed that additional reaction catalyzing the unsaturated bonds to destroy the conjugated system by keratinase, weakening the chromogenic group of melanoidins. Accordingly, this work is meaningful to the industrial decolorization of molasses wastewater.