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Isolation and Properties of Xyloglucanases of Penicillium sp.

O. A. Sinitsyna1*, E. A. Fedorova1, A. G. Pravilnikov1,2, A. M. Rozhkova2, A. A. Skomarovsky3, V. Yu. Matys4, T. M. Bubnova4, O. N. Okunev4, Yu. P. Vinetsky, and A. P. Sinitsyn1,2

1Chemical Faculty, Lomonosov Moscow State University, 119899 Moscow, Russia; fax: (495) 939-0997; E-mail: oasinitsyna@gmail.com

2Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33/2, 119071 Moscow, Russia; fax: (495) 954-2732

3BioChemMack JSC, Leninskie Gory 1/11, 119992 Moscow, Russia; fax: (495) 939-5967

4Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia; fax: (495) 923-3602

* To whom correspondence should be addressed.

Received April 30, 2009; Revision received June 2, 2009
Using chromatographic technique, xyloglucanase (XG) A (25 kDa, pI 3.5, 12th glycosyl hydrolase family) was isolated from the enzyme complex secreted by the mycelial fungus Penicillium canescens, and xyloglucanases XG 25 (25 kDa, pI 4.1, 12th glycosyl hydrolase family) and XG 70 (70 kDa, pI 3.5, 74th glycosyl hydrolase family) were isolated from the enzyme complex of Penicillium verruculosum. Properties of the isolated enzymes (substrate specificity, optimal ranges of pH and temperature for enzyme activity and stability, effect of metal ions on catalytic activity) were compared with the properties of xyloglucanases XG 32 of Aspergillus japonicus, XG 78 of Chrysosporium lucknowense, and XG of Trichoderma reesei. The gene xegA encoding XG A of P. canescens was isolated, and the amino acid sequence of the corresponding protein was determined.
KEY WORDS: xyloglucanase, xyloglucan, Penicillium canescens, Penicillium verruculosum

DOI: 10.1134/S0006297910010062