Isolation and Properties of Major Components of Penicillium canescens Extracellular Enzyme Complex

O. A. Sinitsyna^1*, F. E. Bukhtoyarov¹, A. V. Gusakov¹, O. N. Okunev², A. O. Bekkarevitch², Yu. P. Vinetsky³, and A. P. Sinitsyn¹

¹Faculty of Chemistry, Lomonosov Moscow State University, Moscow 119992, Russia; fax: (7-095) 939-0997; E-mail: oasinitsyna@enzyme.chem.msu.ru

²Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino 142292, Moscow Region, Russia; fax: (7-095) 923-3602

³Institute of Genetics and Selection of Industrial Microorganisms, I Dorozhnyi Proezd 1, Moscow 113545, Russia

^* To whom correspondence should be addressed.

Received March 7, 2003; Revision received April 28, 2003

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The composition of the enzyme complex secreted by Penicillium canescens was investigated. A scheme for purification of the main components of the complex by chromatofocusing on a Mono P column was developed. It was found that along with beta-galactosidase, the major components of the complex were endo-beta-1,4-xylanase (31 kD, pI 8.2-9.3), alpha-L-arabinofuranosidase (60 kD, pI 7.6), arabinoxylan-arabinofuranohydrolase (70 kD, pI 3.8-4.0), and endo-beta-1,3/1,4-glucanase (40 kD, pI 4.4). The substrate specificity, pH and temperature activity optima, adsorbability, thermal stability, and ability for synergic interaction of the isolated enzymes were studied.

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KEY WORDS: Penicillium canescens, endo-beta-1,4-xylanase, alpha-L-arabinofuranosidase, arabinoxylan-arabinofuranohydrolase, endo-beta-1,3/1,4-glucanase, chromatofocusing

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