Abstract
AbstractEffects of process parameters like enzyme concentration, concentration and type of substrate, pH, temperature, speed of agitation, and pressure on lipase catalysis are reviewed. The enzyme concentration controls its interfacial presence and consequently the rate of reaction. A change in substrate concentration alters lipase kinetics. Substrate‐lipase interaction varies with substrate type and pH. Water concentration and agitation affect the extent of interfacial area. Temperature impacts the rate and thermal denaturation of enzymes. Statistical optimization can solve the problem of controlling a variable's effect by other variables. Immobilization support and nonionic surfactant altered the significance of enzyme concentration. The lipase type controlled the impact of concentrations of enzyme, substrate, and water. The water content was important during lipase‐catalyzed hydrolysis and esterification. The mode of agitation influenced the significance of enzyme concentration and temperature. Time had a remarkable impact during hydrolysis. Temperature, substrate type, and chain length notably controlled kinetic parameters. This work paves the way for similar studies on other enzymes.
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