Bioethanol produced from lignocellulosic biomass is regarded as a clean and sustainable energy source. The recalcitrant structure of lignocellulose is a major drawback to affordable bioethanol production from plant biomass. In this study, a novel endo-1,4-xylanase, named Xyn-2, from the camel rumen metagenome, was characterized and evaluated for hydrolysis of agricultural wastes. The enzyme was identified as a psychrohalophilic xylanase with maximum activity at 20 °C, keeping 58% of the activity at 0 °C, and exhibiting twice as much activity in 0.5–4 M NaCl concentrations. Xyn-2 was able to hydrolyze wheat bran (100%), sunflower-seed shell (70%), wheat straw (56%), rice straw (56%), and rice bran (41%), in the relative order of efficiency. Besides, the ethanologenic B. subtilis AP was evaluated without and with Xyn-2 for bioethanol production from wheat bran. The strain was able to produce 5.5 g/L ethanol with a yield of 22.6% in consolidated bioprocessing (CBP). The contribution of Xyn-2 to ethanol production of B. subtilis AP was studied in an SSF system (simultaneous saccharification and fermentation) giving rise to a significant increase in ethanol production (p ≤ 0.001) to a final concentration of 7.3 g/L with a yield of 26.8%. The results revealed that the camel rumen metagenome might be an invaluable source of novel xylanolytic enzymes with potential application in lignocellulosic biomass valorization. At the same time, the results suggest that B. subtilis with a diverse carbon-source preference and sophisticated systems for production and secretion of enzymes might be a promising candidate for strain development for bioethanol production from plant biomass. It might be assumed that the fortification of B. subtilis enzymatic arsenal with select xylanolytic enzymes from camel rumen metagenome may have a great impact on bioethanol production.

Some new linear 3 and 5-step methods for solving special third order ordinary differential equations directly are constructed using Taylor's series expansion. A set of test problems are solved using the new method and the results are compared when the problem is reduced to a system of first order ordinary differential equations and then using the existing Runge-Kutta method. The numerical results have clearly shown the advantage and competency of the new methods.

Xylanase is one of the essential enzymes in divergent industries such as Pulp bleaching, cosmetics, and beverages. It has been widely used in food and pharmaceutical industries and obtained from bacteria, fungi, and crustaceans that is mainly responsible for the hydrolysis of β-1,4 bonds in xylan polysaccharides. Structural and bioinformatics studies of xylanase, can be a contributory and effective aspect of enzyme metabolism and function in polysaccharide components hydrolases. Multiple methods and bioinformatical tools have been used in this study to achieve the whole enzyme structure. The exact enzyme location in the membrane and the main amino acid in the catalytic site have been obtained using computational approaches. This study covers some subjects as enzyme modeling, simulation, structural alignment with similar enzymes, and even docking analysis.