著者
AOSHIMA Ikuko TOZAWA Yukiko OHMOMO Sadahiro UEDA Kiyomoto
出版者
Japan Society for Bioscience, Biotechnology, and Agrochemistry
雑誌
Agricultural and Biological Chemistry (ISSN:00021369)
巻号頁・発行日
vol.49, no.7, pp.2041-2045, 1985
被引用文献数
9 29

The distribution of molasses pigment (melanoidin) decolorizing activity (MDA) was investigated in various Basidiomycetes. MDA was only found in some genera of the white-rot-fungi group of which <i>Coriolus versicolor</i> Ps4a showed high activity, a decolorization yield of approximately 80% under the optimal conditions. Production of MDA by <i>C. versicolor</i> was almost completely coincident with the growth of mycelia. The main MDA was due to intracellular enzymes and induced by the molasses pigment. The induced enzyme consisted of two types, namely a sugar dependent enzyme and a sugar independent enzyme. The decolorization by <i>C. versicolor</i> was due to the decomposition of the molasses pigment.
著者
OHMOMO Sadahiro AOSHIMA Ikuko TOZAWA Yukiko SAKURADA Noriko UEDA Kiyomoto
出版者
Japan Society for Bioscience, Biotechnology, and Agrochemistry
雑誌
Agricultural and Biological Chemistry (ISSN:00021369)
巻号頁・発行日
vol.49, no.7, pp.2047-2053, 1985
被引用文献数
11 19

Melanoidin decolorizing enzymes (MDE) were extracted from mycelia of <i>Coriolus versicolor</i> 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 O<sub>2</sub> for the appearance of the activity, and was inhibited by <i>p</i>-CMB, <i>N</i>-BSI, Ag<sup>+</sup> and <i>o</i>-phenanthroline.<br> 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 O<sub>2</sub>, and was inhibited weakly by Ag<sup>+</sup>, <i>p</i>-CME and <i>N</i>-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.<br> Incidentally, a multiplicative effect between P-III and P-IV for decolorization was observed.