[Back to Issue 4 ToC] [Back to Journal Contents] [Back to Biochemistry (Moscow) Home page]

Heterologous Expression of Thermogutta terrifontis Endo-Xanthanase in Penicillium verruculosum, Isolation and Primary Characterization of the Enzyme

Yury A. Denisenko1,a*, Olga G. Korotkova1, Ivan N. Zorov1,2, Alexandra M. Rozhkova1, Margarita V. Semenova1, Alexandr G. Elcheninov1, Ilya V. Kublanov1, and Arkady P. Sinitsyn1,2

1Federal Research Center “Fundamentals of Fundamental Biotechnology”, Russian Academy of Sciences, 119071 Moscow, Russia

2Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia

* To whom correspondence should be addressed.

Received November 10, 2020; Revised December 29, 2020; Accepted December 29, 2020
Heterologous endo-xanthanase (EX) from the thermophilic planktomycete Thermogutta terrifontis strain was obtained using Penicillium verruculosum 537 (ΔniaD) expression system with the cellobiohydrolase 1 gene promoter. Homogeneous EX with a molecular weight of 23.7 kDa (pI 6.5) was isolated using liquid chromatography methods. This xanthan degrading enzyme also possesses the enzymatic activity towards CM-cellulose, β-glucan, curdlan, lichenan, laminarin, galactomannan, xyloglucan but not towards p-nitrophenyl derivatives of β-D-glucose, mannose and cellobiose. The temperature and pH optima of EX were 55°C and 4.0, respectively; the enzyme exhibited 90% of its maximum activity in the temperature range 50-60°C and pH 3-5.
KEY WORDS: endo-xanthanase, Thermogutta terrifontis, Penicillium verruculosum, heterologous expression, xanthan destruction

DOI: 10.1134/S000629792104009X