Purification and Properties of Two Endo-Type Cellulases from Irpex lacteus (Polyporus tulipiferae)

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概要

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• Two endo-type cellulases, E_2-A and E_2B, were purified from Driselase, a commercial enzyme preparation from Irpex lacteus (Polyporus tulipiferae). Each cellulase showed a single peak on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The specific activities of E_2-A for carboxymethyl cellulose and Avicel were 0.092 and 0.016,and those of E_2-B werer 76.4 and 0.039,respectively. The randomness of E_2-A for the hydrolysis of carboxymethyl cellulose was relatively low while its randomness for the hydrolysis of cotton and viscose rayon was relatively high in contrast to the endo-cellulase of the so far called "Avicelase" type. E_2-B more or less resembled the endo-cellulases of the so far called "CMCase" type, but it was free of β-xylanase activity as E_2-A was. Thus, the two cellulases were different from the Irpex endo-cellulases previously reported.

• 公益社団法人日本生物工学会の論文
• 1983-08-25

著者

• NISIZAWA KAZUTOSI

  Department of Fisheries, College of Agriculture and Veterinary Medicine, Nihon University

• Nisizawa Kazutosi

  Department Of Botany Faculty Of Science Tokyo Kyoiku University

• KUBO KIYOAKI

  Department of Fisheries, College of Agriculture and Veterinary Medicine, Nihon University

• Kubo Kiyoaki

  Department Of Fisheries College Of Agriculture And Veterinary Medicine Nihon University

関連論文

• Action of Exo- and Endo-Type Cellulases from Irpex lacteus on Valonia Cellulose
• Enzymes involved in the last steps of the biosynthesis of mannitol in brown algae
• The enzyme system for the entrance of ^CO_2 in the dark CO_2-fixation of brown algae
• Isolation of a Complex of Endo-cellulases from the Gastric Teeth of Dolabella auricularia by Affinity Chromatography(Biological Chemistry)
• Purification and Properties of Two Endo-Type Cellulases from Irpex lacteus (Polyporus tulipiferae)

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