アメフラシの肝膵臓に含まれるセルラーゼ(予報)

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Cellulase activity has been found in the hepatopancreas of a sea-hare, Aplysia kurodai. The hepatopancreas was homogenized with 0.007M phosphate buffer (pH 7.6), and centrifuged at 5,000g at 0℃. The supernatant was lyophilized and the enzyme was extracted with 0.01M phosphate buffer (pH 6.0). It was salted out with 0.7 saturation of ammonium sulphate, and dialyzed against deionized water. Cellulase activity toward CMC (carboxymethylcellulose) was expressed in terms of reducing sugars, which were measured with Somogyi-Nelson method. CMC cellulase thus purified was found to have an optimal pH at 6.0, an optimal temperature at 40℃, and Km (Michaelis constant) was 0.08%. Three protein fractions have been separated throngh a DEAE-cellulose column by applying NaCl concentration gradient for elution (0→0.14M). The absorbance of protein was measured both by O.D. at 280mμ and at 750mμ. The first peak in the eluate was found not to contain cellulase activity, and the second one was the fraction with a remarkable cellulase activity. The last peak was an enzymatically inactive fraction with the absorbance at 280mμ, but without any at 750mμ. The molecular weight of the CMC cellulase in Aplysia was estimated to be approximately 50,000 through gel filtration of Sephadex G-75. Together with cellulase activity, alginase activity was also detected in the hepatopancreas by a determination of viscosity decrease of alginic acid and by a production of reducing sugars.
社団法人日本動物学会の論文
1968-05-15

アメフラシの肝膵臓に含まれるセルラーゼ(予報)

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