The diversity of the biotechnological applications of chitinolytic enzymes requires different enzyme-producing strains with different properties suitable for each process. In this work the chitinase encoded by the chiA gene of Bacillus halodurans has been studied. The protein shows a modular structure characterized by the catalytic domain of glycosyl hydrolases family 18 (GH18), fibronectin type III domain (FnIIID) and a carbohydrate-binding module family 5 (CBM5). The expression of the gene in Escherichia coli has made it possible to demonstrate the functionality of the protein which is active in the temperature range of 5-55 degrees C and pH values of 5.5-8.5 while maintaining a high stability under suboptimal conditions. The enzyme hydrolyzes colloidal chitin and different p-NP(GlcNAc)(n) (n = 1-3) by an "-exo" type mechanism according to the information deduced from its sequence. The production of the protein was optimized by constructing recombinant strains, and the effect of the expression vector used, the cell density of the culture, the concentration of inducer and the induction time were studied. Based on its spectrum of activity, stability and mechanism of action, it arises as an enzyme of potential interest for production of N-acetyglucosamine or conversion of chitin into biologically active chito-oligosaccharides. (C) 2014 Elsevier Ltd. All rights reserved.