Catalase from Salinococcus roseus, a potential enzyme for industrial uses

Catalases are enzymes widely used in industrial applications, and their stability under extreme conditions generates significant interest. In this study, with the aim of evaluating the potential source of robust enzymes, the purification and biochemical and structural characterization of catalase from Salinococcus roseus have been performed. The catalase from S. roseus, a Gram-positive halotolerant bacterium capable of growing in environments containing up to 25% NaCl, was purified using chromatographic techniques, reaching a purity of 75.8%. The presence of the heme group was confirmed by UV-Vis spectroscopy, and a monomeric mass of 74.6 kDa was estimated. The structural model was studied by generating a homology model using templates from Salinicoccus cyprini and Escherichia coli. Kinetically, the enzyme exhibited Michaelis-Menten behavior (k_cat = 7.19 × 10⁵ s^-1, K_m = 35.6 mM). Compared to catalases from Aspergillus niger and bovine liver, the S. roseus enzyme showed considerable thermal stability (60% activity at 75 °C), a broad pH activity range (up to pH 11), and moderate salt tolerance. A catalase source from bacteria, easily cultivated and showing good thermostability and high catalytic activity at high salt concentrations, highlights its biotechnological potential for industrial processes requiring extreme temperatures, salt, and pH conditions.