5) Aspergillus saitoiの生産するセルロース分解酵素の研究(第2報) : Carboxymethylcellulaseの精製とその結晶化

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In previous papers, some action of cellulolytic enzymes obtained from Aspergillus Saitoi has been studied through the use of various substrated ie., swollen cellulose, sodium carboxymethyl cellulose and salicin.The present paper is concerned with the isolation of an enzyme of carboxymethyl-cellulases among the main enzyme products from Asp. Saitoi, its purification and the characterization of its property.The cellulase in the culture filtrate of Asp. Saitoi was purified successively through a sequence of concentration, reprecipitation with ammonium sulfate, decolorization with active carbon, the removal of salts with Sephadex G-75 and by fractionation with an ion exchange resin(Amberlite IRG-50). The concentration by polyethylenglycol(Carbowax-1500) and finally the crystallization with an addition of acetone completed the purification. The crystalline carboxymethylcellulase was electrophoretically homogeneous, the yield of this enzyme was 0.34 percent and the specific activity was increased twenty fold as compared with the starting material. The crystalline carboxymethylcellulase exhibited a specific high activity for carboxymethyl cellulose, although it did not attack cellulose powder or swollen cellulose and cellobiose or salicin and other similar substance. The maximal ultraviolet absorption of the carboxymethylcellulase was at 278mμ. The K_m of the enzyme-substrate complex was found to be 6.5756g/L. The isoelectric point of this enzyme was a pH of 5.2-5.3.
社団法人日本生物工学会の論文
1963-03-15

5) Aspergillus saitoiの生産するセルロース分解酵素の研究(第2報) : Carboxymethylcellulaseの精製とその結晶化

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