Isolation and Properties of Recombinant Inulinases from Aspergillus sp.

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P. V. Volkov¹, O. A. Sinitsyna^1,2*, E. A. Fedorova¹, A. M. Rojkova¹, A. D. Satrutdinov¹, I. N. Zorov^1,2, O. N. Okunev³, A. V. Gusakov^1,2, and A. P. Sinitsyn^1,2

¹Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33/2, 119071 Moscow, Russia; fax: (495) 954-2732

²Faculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: (495) 939-0997; E-mail: oasinitsyna@gmail.com

³Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, pr. Nauki, 142292 Pushchino, Moscow Region, Russia; fax: (495) 923-3602

^* To whom correspondence should be addressed.

Received December 7, 2011; Revision received January 17, 2012

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The genes inuA and inu1, encoding two inulinases (32nd glycosyl hydrolase family) from filamentous fungi Aspergillus niger and A. awamori, were cloned into Penicillium canescens recombinant strain. Using chromatographic techniques, endoinulinase InuA (56 kDa, pI 3) and exoinulinase Inu1 (60 kDa, pI 4.3) were purified to homogeneity from the enzymatic complexes of P. canescens new transformants. The properties, such as substrate specificity, pH- and T-optima of activity, stability at different temperatures, influence of cations and anions on the catalytic activity, etc., of both recombinant inulinases were studied.

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KEY WORDS: inulin, endoinulinase, exoinulinase, Penicillium canescens, Aspergillus niger, Aspergillus awamori

DOI: 10.1134/S0006297912050094

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