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Obtainment of a Complex Enzyme Preparation with Enhanced Pectinase Activity Based on the New Mutant Strain T. reesei Co-44

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Abstract

Studies were conducted to obtain a complex enzyme preparation that allows efficient hydrolysis of the main plant nonstarch polysaccharides (cellulose, xylans, and pectin). The goal of the studies was to optimize the composition of a fermentation medium for the submerged cultivation of the new mutant strain T. reesei Co-44, a highly active producer of endo-carbohydrases. A concentrate of low molecular soy components was chosen as the inducer of the key carbohydrase biosynthesis by the strain. This concentrate provided the maximum (more than eightfold) increase in polygalacturonase activity and an increased level of endoglucanase and xylanase biosynthesis. After the cultivation of T. reesei Co-44 under optimized conditions, a complex enzyme preparation, Xylorizin K4, was obtained, and its physicochemical properties were studied. The presence of endopolygalacturonase (GH28) T. reesei in Xylorizin K4 was confirmed via electrophoresis and MALDI⎯TOF mass spectrometry. The studies show the potential of Xylorizin K4 application for the production of soy-protein concentrates to eliminate the main soybean nonstarch polysaccharides.

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ACKNOWLEDGMENTS

The equipment of the Industrial Biotechnology Center for Collective Use of the Fundamentals of Biotechnology Federal Research Center of the Russian Academy of Sciences was used in this work.

Funding

This work was carried out within the framework of the Program of Basic Scientific Research of the State Academies of Sciences for 2019–2021 (topic no. 0529-2019-0066).

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Correspondence to E. V. Kostyleva.

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The authors declare that they have no conflict of interest. This article does not contain any research involving humans or animals as research objects.

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Translated by P. Kuchina

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Kostyleva, E.V., Sereda, A.S., Velikoretskaya, I.A. et al. Obtainment of a Complex Enzyme Preparation with Enhanced Pectinase Activity Based on the New Mutant Strain T. reesei Co-44. Appl Biochem Microbiol 57, 94–101 (2021). https://doi.org/10.1134/S0003683821010130

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