Purification and Some Properties of Melanoidin Decolorizing Enzymes, P-III and P-IV, from Mycelia of Coriolus versicolor Ps4a

Abstract

Melanoidin decolorizing enzymes (MDE) were extracted from mycelia of Coriolus versicolor Ps4a and purified by DEAE-Sephadex, DEAE-Sephacel and Sephadex G-200 column chromatographies. MDE of this strain consisted of a main fraction, P-fraction, and a minor fraction, E-fraction, and the P-fraction was composed of at least five enzymes. P-III and P-IV in the P-fraction were picked as typical enzymes of this strain, and their enzymatic properties were investigated. P-III had a molecular weight of 48,400 ~ 50,000, an optimum pH of 5.5 and an optimum temperature of 30~35°C. P-III required glucose and O2for the appearance of the activity, and was inhibited by p-CMB, Ar-BSI, Ag+and 0-phenanthroline. On the other hand, P-IV had a molecular weight of 43,800 ~ 45,000, an optimum pH of 4.0~4.5 and an optimum temperature of 30~35°C. P-IV could decolorize melanoidin in the absence of glucose and O2, and was inhibited weakly by Ag+, p-CMB and N-BSI. P-IV is the enzyme that attacks the melanoidin directly in comparison with P-III which attacks melanoidin indirectly as in the sub-reaction of sugar oxidase. Incidentally, a multiplicative effect between P-III and P-IV for decolorization was observed. © 1985, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.