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This study aimed to produce and nanoconjugated the xylanase enzyme of Bacillus subtilis BTX6 (MH101286) isolated from geothermal hot springs in Diyadin, Agri (Davud). Within the scope of this study, the 1,4-β-endo xylanase (GH11 family) free enzyme from B. subtilis was cloned, recombinantly expressed in E. coli after that nanoconjugated by encapsulation with the Anadoluca method. Then, the recombinantly produced enzyme and the nanoconjugated enzyme were characterized. According to the results, the optimum activity of both recombinant enzyme and nanoconjugated xylanase enzyme were determined as pH 7.0. Considering the optimal temperature values, it was determined that the recombinant enzyme display optimum activity at 68 °C, while the nanoconjugated enzyme shows the best activity at 75 °C. The molecular weight of the recombinantly produced enzyme was measured as 71 kDa. In the enzyme activity measurements, the recombinant enzyme was determined as 1803 U/mg., and the activity of the nanoconjugated enzyme was determined as 1898 U/mg. Some metal ions such as MgSO 4 , CuSO 4 , CaCl 2 , ZnSO 4, and FeSO 4 increased the activity of recombinant and nanoconjugated enzymes. The K m value for the recombinant enzyme was 2.298 (mM), the V max value was 5.691 (U/mg.). Nanoconjugated enzyme the enzyme increased K m (2.298–2.402 mM) and V max (5.691–6.195 U/mg.) values. As a result, it was concluded that the cloning and nanoconjugated xylanase enzyme methods preferred in this study can be used effectively to improve enzyme activity in industrial processes. [Display omitted] • Xylanase enzyme was recombinantly produced from the highly active isolate. • Endo-xylanase gene from Bacillus subtilis BTX6 (MH101286) was clonned and overexpressed. • Anadoluca method was used for the nanoconjugated of the xylanase enzyme. • Nanoconjugated enzyme was more stable than the free enzyme in higher temperatures. [ABSTRACT FROM AUTHOR]