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Research article2014Peer reviewed

The production of highly effective enzyme complexes of cellulases and hemicellulases based on the Penicillium verruculosum strain for the hydrolysis of plant raw materials

Sinitsyn, A. P.; Osipov, D. O.; Rozhkova, A. M.; Bushina, E. V.; Dotsenko, G. S.; Sinitsyna, O. A.; Kondrat'eva, E. G.; Zorov, I. N.; Okunev, O. N.; Nemashkalov, V. A.; Matys, V. Yu.; Koshelev, A. V.

Abstract

Methods for the production and analysis of cellulase and hemicellulase enzyme preparations of various compositions based on the Penicillium verruculosum carbohydrase complex and intended for the effective hydrolysis of different types of cellulose-containing materials (CCMs) have been developed. New recombinant strains of P. verruculosum producing multienzyme carbohydrase complexes with increased activities of cellulases (due to the expression of endo-beta-1,4-glucanases I and IV and cellobiohydrolase II from Trichoderma reesei) and hemicellulases (due to the expression of endo-beta-1,4-xylanases from P. canescens and T. reesei and endo-beta-1,4-mannanase from T. reesei) were constructed. The hydrolytic efficiency of the enzyme preparations (EPs) produced by the new recombinant strains during continuous hydrolysis of three CCM types (milled aspen, depitched pine wood, and milled bagasse) was studied. It was shown that new EPs containing recombinant proteins and retaining their own basic cellulase complex are characterized by the highest hydrolytic ability, exceeding that of the EP based on the original P. verruculosum strain. The recombinant enzyme preparations were highly stable; the optimal pH and temperature values for cellulase, xylanase and mannanase activities were in the range of 3.5-5.5 and 50-80A degrees C, respectively.

Keywords

cellulases; cellulose-containing materials; enzymatic hydrolysis; hemicellulases; Penicillium verruculosum

Published in

Applied Biochemistry and Microbiology / Prikladnaya Biokhimiya i Mikrobiologiya
2014, Volume: 50, number: 8, pages: 761-772

    UKÄ Subject classification

    Biocatalysis and Enzyme Technology

    Publication identifier

    DOI: https://doi.org/10.1134/S0003683814080055

    Permanent link to this page (URI)

    https://res.slu.se/id/publ/84287