Immobilization and enzymatic kinetic study of protease on chitosan nanoparticles

The immobilization of protease on chitosan nanoparticles was systematically examined to augment enzymatic stability and catalytic efficiency. Chitosan nanoparticles were synthesized through the method of ionic gelation and subsequently utilized as a substrate for enzyme adsorption. The kinetic parameters of both free and immobilized protease was assessed employing the Michaelis-Menten and Lineweaver-Burk kinetic models. The immobilized protease displayed an elevated maximum velocity (Vmax = ۶۸.۵۴ U/mL) in contrast to the free enzyme (Vmax ۶۰.۰۳ U/mL) and a reduced Michaelis constant (Km ۲.۵۱ mg/mL versus ۲.۳۶ mg/mL). In addition, the immobilized enzyme exhibited an expanded pH range (۳-۹) for activity alongside thermal stability. So that the immobilized enzyme has more relative activity than the free state at acidic and basic pHs. These results substantiate that chitosan nanoparticles function as an efficacious support for protease immobilization, signifying an enhanced substrate affinity and improved stability, thereby enhancing both operational stability and enzymatic performance, which holds significant promise for biocatalytic applications in an industrial context.

کلیدواژه ها:

Chitosan nanoparticles ، Enzyme immobilization ، Protease ، Thermal stability ، Michaelis-Menten kinetics