The hydrolytic enzyme xylanase is a chemically relevant enzyme that has broad industrial applications including pulp and paper, food and feed, textile, and biofuels industry. However, the bioactivity and stability of the enzyme have historically been affected by some factors, e. g. its ability to be reused, its operational durability in harsh processing conditions, and its use as a catalyst under very severe conditions. Immobilization techniques are useful as possible approaches to enhance the thermal and operational stability of xylanase and allow repeated use of the enzyme, as well as maintain degradation efficiency over long periods of time. This review (or study) reviews various immobilization techniques, including adsorption, covalent binding, entrapment, and encapsulation, as well as their ability to modify the biochemical properties of the enzyme. The bioactivity of the enzyme with respect to supportive material effects, such as natural polymers, synthetic matrices, and nanomaterials, are investigated critically. Finally, the latest progress in the methods of stabilization of xylanase is discussed, including genetic engineering, cross-linking, and additives for building resistance to denaturation.