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      • 忠南大學校 理科大學 微生物學科

        李基朋,李榮河 忠南大學校 環境問題硏究所 1986 環境硏究 Vol.4 No.2

        The specificity of induction of cellulose-and xylan-degrading enzymes in Aspergillus nidulans was investigated using various cellulosic and hemicellulosic substrates as carbon sources. Even though A. nidulans was stimulated in growth when the organism was grown on glucose and other readily metabolizable substrates, the biosynthesis of cellulase and xylanase complexes was not clearly correlated with the growth. The most potent inducers for cellulase and xylanase complexes were carboxymethylcellulose for endoglucanase, cellobiose for β-glucosidase, and xylan for endoxylanase and β-xylosidase. The mixtures of these inducers, however, were much more effective not only for the enhancement of the biosynthesis of all cellulase and xylanase complexes but also for the balanced production of these enzyme components than individual inducers. These substrate synergisms suggest that the biosynthes is of cellulase and xylanase complexes in A. nidulans is regulated in coordination at the level of induction.

      • Adsorption and Activity of Carboxymetylcellulase on Clay Minerals

        Rhee,Kee Bung,Rhee,Young Ha 忠南大學校 環境問題硏究所 1985 環境硏究 Vol.3 No.2

        Most of abiontic soil carboxymethylcellulase (CMCase) actiivities were located in clay and silt frac- tions, but CMCase holding capacity of clay fraction was by far greater than that of silt fraction, The adsorption of CMCase on kaolinite was found to be pH dependent and maximum adsorption occurred at or below the isoelectric point (pI) of this enzyme. Adsorption of CMCase on clay minerals appeared to result in a severe loss of activity. A competition between CMCase and substrate for binding to clay minerals was an obstacle for rapid enzymatic biodegradation of substrate. CMCase adsorbed on clay tion to the surface area and cation- exchange capacity of clays. Most of abiontic soil carboxymethylcellulase (CMCase) actiivities were located in clay and silt fractions, but CMCase holding capacity of clay fraction was by far greater than that of silt fraction, The adsorption of CMCase on kaolinite was found to be pH dependent and maximum adsorption occurred at or below the isoelectric point (pI) of this enzyme. Adsorption of CMCase on clay minerals appeared to result in a severe loss of activity. A competition between CMCase and substrate for binding to clay minerals was an obstacle for rapid enzymatic biodegradation of substrate. CMCase adsorbed on clay minerals showed the inhanced thermostability and shift of pH optima,and these trends were in proportion to the surface area and cation- exchange capacity of clays.

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