Hydrolysis and adsorption reversibility experiments were run for initial enzyme activity of 4.48, 9.65, 11.19 and 17.14U/mL at a temperature 30$^circ C$. The chitin particle size corresponded to a mean particle diameter of 0.127mm, and the initial concentration of chitin was 10mg/mL. After approximately 2hrs, the enzyme activity remained constant in a speudo-steady state. The amounts in the bulk [E] and the amounts of enzyme adsorbed on the chitin surface [E] are plotted on Lineweaver-Burk plot to yield a linear relationship with a correlation coefficient of 0.99, a slope of 2.79cm$^-1$ and an intercept of 0.08$ extrm{cm}^2$/U. From this parameters, the values of [E$_T$] and $K_E$ were calculated to be 12.5U/cm$^2$ and 34.88U/mL. respectively, Adsorption isotherm of the enzyme on the particles showed a well developed plateau of 1.35$ imes$10$^-3$, 4.72$ imes$10$^-3$, 4.42$ imes$10$^-3$, 8.58$ imes$10$^-3$U/cm$^2$ at 30$^circ C$. To determine the specificity of chitinase for crystalline chitin, the free energy of adsorption was measured, and its was determined as about -14.62~-18.8kJ/mol.