Characterization of Xylanase enzyme from Neocallimastix sp.'s isolated from mountain goats in tunceli

Numerous fungal enzymes have been identified from nature that continue to drive strain engineering and bioprocessing for a variety of industries. However, while a number of branches have been explored, the vast majority of the fungal kingdom remains unexplored for industrial applications. Anaerobic fungi, such as Neocallimastigomycota, have recently been found to harbor the greatest diversity of biomass-degrading enzymes among the fungal kingdom. Anaerobic fungi (AF) are rare organisms that play a role in the digestion of lignocellulosic biomass, which is a renewable energy source in nature. Rumen fungi, which are important in terms of biotechnological applications, were isolated from stool samples of Anatolian Wild Goats (Bezoar-Capra aegagrus) distributed in Tunceli, morphologically at genus level Neocallimastix spp. has been defined as. Among these isolates, those with high enzyme activity (DAF1, DAF2 and DAF3) were selected and used in other analyzes. The thermal stability of the enzymes was determined with the optimum pH, temperature, incubation times of xylanase, lichenase and carboxymethyl cellulase enzymes. Enzyme activities were found to be highly extracellular. The optimum pH and temperature for enzyme activity were determined as 6 and 50°C, respectively, in the isolates using xylan. The specific activity for xylanases of the isolates (DAF1, DAF2 and DAF3) grown in straw medium was found to be 499±19.29, 560.42±9.39 and 513.01±29.22 μmol/min/ml, respectively. In addition, 1 mM concentrations of metal ions used in the study have been shown to have a positive effect on enzyme activity.