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

Heterologous endo-xanthanase (EX) from the thermophilic planktomycete Thermogutta terrifontis strain was obtained using Penicillium verruculosum 537 (Delta niaD) 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, beta-glucan, curdlan, lichenan, laminarin, galactomannan, xyloglucan but not towards p-nitrophenyl derivatives of beta-D-glucose, mannose and cellobiose. The temperature and pH optima of EX were 55 degrees C and 4.0, respectively; the enzyme exhibited 90% of its maximum activity in the temperature range 50-60 degrees C and pH 3-5.

Automated summary

Heterologous endo-xanthanase (EX) was obtained from Thermogutta terrifontis strain using a fungal expression system with a high molecular weight and activity towards various polysaccharides. The enzyme showed optimal activity at 55 degrees C and pH 4.0, with 90% activity retained in the temperature range of 50-60 degrees C and pH range of 3-5.