Cellulase Complex from Chaetomium cellulolyticum: Isolation and Properties of Major Components

N. V. Ankudimova^1*, V. A. Baraznenok¹, E. G. Becker¹, and O. N. Okunev²

¹Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-0997; E-mail: ankudimova@enzyme.chem.msu.ru

²Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia; fax: (095) 923-3602; E-mail: okunev@ibpm.serpukhov.su

^* To whom correspondence should be addressed.

Received January 25, 1999; Revision received March 10, 1999

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Four major components of the cellulase complex of Chaetomium cellulolyticum have been isolated by gel-filtration, ion-exchange chromatography on DEAE-Toyopearl and Macro Prep Q, and chromatofocusing on Mono P. These components include three endoglucanases (19, 35, and 40 kD) and a cellobiohydrolase (45 kD). The isoelectric points of the enzymes vary from 3.8 to 4.2. The optimal pH values for catalytic activity are in the range 4.5-6.0, and the optimal temperatures are in the range 60-70°C. Of these enzymes the 19 kD endoglucanase is the most stable; it retained high activity within a broad pH range (from 5.0 to 9.6) at 50°C for 3 h. This enzyme also had the highest topolytic activity determined by the efficiency of removal of indigo from the surface of cotton.

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KEY WORDS: cellulase, endoglucanase, cellobiohydrolase, purification, biological bleaching

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