Application of The Immobilization Method for Obtaining Serratiopeptidase With Prolonged Action
Abstract
The present study investigates the possibility of using an immobilization method based on polyaldehyde dextran (PAD) to enhance the stability of serratiopeptidase (SP). Serratiopeptidase, a proteolytic enzyme, possesses a broad spectrum of biological activity; however, its practical application is limited due to low stability under external conditions. Dextran was functionalized by periodate oxidation to generate reactive aldehyde groups capable of forming covalent bonds with protein amino groups via Schiff base formation. Prolongation and stable preservation of serratiopeptidase activity were confirmed by evaluating its proteolytic efficiency. Protease activity was determined using a modified method with casein as a substrate. It was established that the immobilized form of serratiopeptidase demonstrates increased catalytic efficiency and reproducibility, making it promising for pharmaceutical applications.