Chitinase (EC 3.2.1.14) plays a crucial role in chitin degradation, specifically breaking down the 1→4 β-glycosidic bonds of N-acetyl-D-glucosamine (GlcNAc) to produce its mono-or oligomers. This study aims to study the characteristics of chitinase from Vibrio sp. (isolated from tiger shrimp in Indonesia) and explore the role of calcium ions (Ca 2+ ) in increasing chitinase activity. The optimum condition for chitinase activities is pH 7.5, 45 o C of temperature, and 120 min of incubation time. The enzyme activity parameters such as K m and V max values were calculated by varying the concentration of Ca 2+ , namely: 0 % ; 0.2 % ; 0.4 %; 0.6% ; 0.8 %. The final product of the chitinase reaction, the GlcNAc, is then used to measure the enzyme activity based on the Somogyi-Nelson method. The results showed that chitinase isolated from Vibrio sp. has increasing activity with the addition of Ca 2+ . Without the addition of Ca 2+ , the K m and V max of chitinase were 7.781 µmol mL -1 and 0.066 µmol min -1 , respectively. The treatment of 0.4 % Ca 2+ shows optimum activity with the K m and V max at 6.723 µmol mL -1 and 0.079 µmol min -1 , respectively. The results showed the potential use of Ca 2+ as a chitinase activator to fulfill demands for energy-efficient and economically profitable chitinase usage.