A rigorous kinetic model describing the stepwise triglyceride hydrolysis at the oil-water interface, based on the Ping Pong Bi Bi mechanism using suspended lipase having positional specificity, was constructed. The preference of the enzyme to cleave to the ester bonds at the edge and the center of the glycerol backbone of the substrates (tri-, di- or monoglyceride) was incorporated in the model. This model was applied to the experimental results for triolein hydrolysis using suspended Porcine pancreatic lipase (an sn-1,3 specific lipase) and Candida rugosa lipase (a non-specific lipase) in a biphasic oil-water system under various operating conditions. In order to discuss the model's advantages, other models that do not consider the positional specificity of the lipase were also applied to our experimental results. The model considering the positional specificity of the lipase gave results which fit better with the experimental data and described the effect of the initial enzyme concentration, the interfacial area, and the initial concentrations of triolein on the entire process of the stepwise triolein hydrolysis. This model also gives a good representation of the rate for cleaving the respective ester bonds of each substrate by each type of lipase.
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