Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 |
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| Authors: | Semia Ellouz Chaabouni Tahar Mechichi Ferid Limam Nejib Marzouki |
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| Affiliation: | (1) National School of Engineers of Sfax, BP W 3038 Stax Cedex, Tunisia;(2) Biotechnology Center of Sfax, BP W 3038 Sfax Cedex, Tunisia;(3) National Institute of Scientific and Technical Research, PB 95, 2050 Hammam-Lif, Tunisia;(4) National Institute of Applied Sciences and Technology, BP 676, 11080 Tunis Cedex, Tunisia |
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| Abstract: | Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol 6 culture medium. The molecular weights of EG A and EG B were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60 degrees C for EG A and 50 degrees C for EG B. EG A was thermostable at 60 degrees C and remained active after 1 h at 70 degrees C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and beta-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations Hg2+, Co2+, and Mn2+. |
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| Keywords: | Penicillium occitanis mutant Pol 6 cellulase endoglucanases purification |
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