Mutations in the protein affect not only the structure of protein, but also its function and stability. Prediction of mutant protein stability with accuracy is desired for uncovering the molecular aspects of diseases and design of novel proteins. Many advanced computational approaches have been developed over the years, to predict the stability and function of a mutated protein. These approaches based on structure, sequence features and combined features (both structure and sequence features) provide reasonably accurate estimation of the impact of amino acid substitution on stability and function of protein. Recently, consensus tools have been developed by incorporating many tools together, which provide single window results for comparison purpose. In this review, a useful guide for the selection of tools that can be employed in predicting mutated proteins' stability and disease causing capability is provided.

Xylanases have a great potential, mainly known for industrial applications. They can hydrolyze the xylose (Hemicellulose of plant cell wall) and can be used for bio-bleaching the kraft pulp. As it reduces the requirement of harsh chemicals in the process, it can be used further to a number of bio-products with a great aggregate value. Microbial-origin xylanases can also be used in improving the nutritional quality of animal feed (e.g. food additives to poultry, piggery or fishery) and indirectly affect the humans. Additionally they can be used directly in human food in bakery, clarification of juices and in xenobiotics like tobacco processing. The great value of xylanase as a bio-bleaching agent has now a new dimension of fiber digesting agent having relevance to food, drugs and cosmetics act. This review presents some important applications of Xylanases extended up to biomedical sciences. [Int J Basic Clin Pharmacol 2013; 2(3.000): 237-246

Xylanase gene isolated from Bacillus brevis was expressed in E. coli BL21. Sequencing of the gene (Gen Bank accession number: HQ179986) showed that it belongs to family 11 xylanases. The recombinant xylanase was predominantly secreted to culture medium and showed mesophilic nature (optimum activity at 55°C and pH 7.0). The cell free culture medium exhibited 30 IU/ml xylanse activity. The enzyme did not show any cellulose activity and was active under wide range of temperature (40°C to 80°C) and pH (4 to 9). The enzyme showed considerable thermo stability and regained over 90% of activity, when returned to 55°C after boiling for 5 min. These physiochemical properties of B. brevis xylanse show high potential of its applications in paper and pulp industry.Electronic supplementary materialThe online version of this article (doi:10.1186/2193-1801-3-20) contains supplementary material, which is available to authorized users.

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