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Identification of Core Cellulolytic Enzymes from the Talaromyces cellulolyticus Strains Y-94 and S6-25

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Abstract

The cellulose-degrading fungus strain Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus) Y-94, which was isolated in 1982 from soil in Japan, and strain S6-25, a derivative of Y-94 with higher cellulase productivity, are fungi that exhibit promise as alternatives to Trichoderma reesei for the industrial production of cellulase. MALDI-TOF MS analysis of the T. cellulolyticus Y-94 protein secretome demonstrated that strain Y-94 expressed and secreted a broad spectrum of proteins for the degradation of hemicellulose, starch, or pectin; these proteins include 2 types of α-L-arabinofuranosidases, 2 types of putative glucoamylases, Streptomyces laminarinase-like protein, mutanase, α-amylase, polysaccharide lyase family 6/pectate lyase 3, and β-N-acetylhexosaminidase. The cellulase system of strain S6-25 had the same cellobiohydrolases (Cel6A and Cel7A), β-glucosidase (Bgl3A), xylanase (Xyl10A), and endoglucanase (Cel5A) as strain CF-2612, another derivative of Y-94. However, instead of Cel7B, S6-25 cells expressed another endoglucanase (Cel5C). Two cellobiohydrolases, Cel7A and Cel6A, represented approximately 60% (wt/wt) of the proteins secreted by the strain and were the main enzymes of the cellulase complex. The increase in cellulase complex activity in the S6-25 strain compared with Y-94 may be explained, at least partly, by the presence of an additional copy of the cel7A gene in the cellular genome, which was confirmed by RT-qPCR analysis.

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Authors and Affiliations

  1. Ajinomoto-Genetika Research Institute, 117545, Moscow, Russia

    L. R. Ptitsyn, T. A. Yampolskaya, E. A. Kutukova & I. B. Altman

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  1. L. R. Ptitsyn
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  2. T. A. Yampolskaya
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  3. E. A. Kutukova
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Correspondence to L. R. Ptitsyn.

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Ptitsyn, L.R., Yampolskaya, T.A., Kutukova, E.A. et al. Identification of Core Cellulolytic Enzymes from the Talaromyces cellulolyticus Strains Y-94 and S6-25. Appl Biochem Microbiol 57 (Suppl 1), S38–S45 (2021). https://doi.org/10.1134/S0003683821100100

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