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