A chitinase (CHT) and a protease (PRO) were purified from the culture supernatant of Serratia sp. TKU017, with shrimp shell as the sole carbon/nitrogen source. The molecular masses of CHT and PRO determined by SDS-PAGE were approximately 65 kDa and 53 kDa, respectively. CHT was inhibited by Mn2+ and Cu2+, and PRO was inhibited by most tested divalent metals and EDTA. The optimum pH, optimum temperature, pH stability, and thermal stability of CHT and PRO were pH 5, 50°C, pH 5-7, and <50oC, and pH 9, 40°C, pH 5-11, and <40°C, respectively. PRO retained 95% of its protease activity in the presence of 0.5 mM SDS. The result demonstrates that PRO is an SDS-resistant protease and probably has a rigid structure. The 4th-day supernatant showed the strongest antioxidant activity (70%, DPPH scavenging ability) and the highest total phenolic content (196±6.2 μg of gallic acid equiv./ml). Significant associations between the antioxidant potency and the total phenolic content, as well as between the antioxidant potency and free amino groups, were found for the supernatant. With this method, we have shown that shrimp shell wastes can be utilized and it is effective in the production of enzymes and antioxidants, facilitating its potential use in industrial applications and functional foods.
All Science Journal Classification (ASJC) codes
- Applied Microbiology and Biotechnology