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Enzymological Properties of Endo-(1–4)-β-Glucanase Eg12p of Penicillium canescens and Characteristics of Structural Gene egl2

A. M. Chulkin1, D. S. Loginov1*, E. A. Vavilova1, A. R. Abyanova1, I. N. Zorov1,2, S. A. Kurzeev1,2, O. V. Koroleva1, and S. V. Benevolenskii1

1Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 117091 Moscow, Russia; fax: (495) 954-2732; E-mail: d.s.loginov@inbi.ras.ru; inbi@inbi.ras.ru

2Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (495) 939-0997; E-mail: info@rector.msu.ru

* To whom correspondence should be addressed.

Received December 3, 2008; Revision received January 15, 2009
Gene egl2 of secreted endo-(1–4)-β-glucanase of glycosyl hydrolase family 5 of the mycelial fungus Penicillium canescens was cloned. The gene was expressed in P. canescens under control of a strong promoter of the bgaS gene encoding β-galactosidase of P. canescens, and endoglucanase producing strains were obtained. Chromatographically purified recombinant 48 kDa protein had pH and temperature optima 3.4 and 60°C, respectively, exhibited specific activity of 33 IU, and had Km and Vmax in CM-cellulose hydrolysis of 10.28 g/liter and 0.26 µmol/sec per mg, respectively.
KEY WORDS: endoglucanase, mycelial fungus, Penicillium canescens, gene

DOI: 10.1134/S0006297909060108