Enzymatic Decolorization of Melanoidin by Coriolus sp. No. 20

Coriolus sp. No. 20 decolorized a melanoidin solution, a decrease of about 80% in darkness under the optimal conditions. This decolorization occurred with an intracellular enzyme which was prepared from an extract of integrated mycelia, and required aeration and some kinds of sugars, particularly glucose and sorbose. The fraction with melanoidin-decolorizing activity was collected and purified by DEAE-cellulose and Sephadex G-200 column chromatographies. The optimal pH and temperature were pH 4.5 and 35°C, respectively. The molecular weight was found to be about 200,000 by SDS-gel electrophoresis. The purified enzyme was identified as sorbose oxidase; decolorization proceeded in the presence of oxygen and sugars such as maltose, sucrose, lactose, galactose and xylose, besides glucose and sorbose. Glucose in the reaction mixture was converted to gluconic acid. Melanoidin was suggested to be decolorized by the active oxygen formed.