Adsorption capacity of chitosan towards toxic p-nitrotoluenosulfonic acid (PNTS) was investigated in this study. An adsorption isotherm was determined at 293 K. The character of the process was specified. On the basis of calorimetric measurements the thermal power of the process was determined. The investigations revealed that chitosan was a good PNTS adsorbent, the adsorption of this compound had a character of chemisorption and took place on the adsorbent surface.

This study aims at the immobilization and characterization of thermoalkalophilic lipases produced recombinantly from Bacillus thermocatenulatus BTL2 and Bacillus pumilus MBB03. For this purpose, immobilization of the produced enzymes in calcium-alginate@gelatin (Ca–Alg@gelatin) hydrogel beads, immobilization optimization and characterization measurements of the immobilized-enzyme hydrogels were conducted. Optimum temperature and pH values were determined for B. thermocatenulatus and B. pumilus MBB03 immobilized-enzyme hydrogels (60–70 °C, 55 °C and pH 9.5, pH 8.5). Thermal stability was determined between 65 °C and 60 °C of B. thermocatenulatus and B. pumilus MBB03 immobilized enzymes, respectively. The pH stability was determined between pH 7.0–11.0 at +4°C and pH 8.0–10.0 at +4 °C, respectively.
In conclusion, the entrapment technique provided controlled production of small diameter hydrogel beads (~ 0:19 and ~ 0:29) with negligible loss of enzyme. These beads retained high lipase activity at high pH and temperature. The activity of Ca–Alg@gelatin-immobilized lipase remained relatively stable for up to three cycles and then markedly decreased. With this enzyme immobilization, it may have a potential for use in esterification and transesterification reactions carried out in organic solvent environments. We can conclude that it is one of the most promising techniques for highly efficient and economically competent biotechnological processes in the field of biotransformation, diagnostics, pharmaceutical, food and detergent industries.