Hashem Nayeri, Ali Fattahi, Marziyeh Iranpoor-mobarakeh, Parivash Nori
Department of Biochemistry, Falavarjan Branch, Islamic Azad University, Isfahan, Iran
Department of Pharmaceutics, School of Pharmacy, Kermanshah University of Medical Sciences, Kermanshah 6734667149, Iran
Department of Biochemistry, Science and Research Branch, Islamic Azad University, Fars, Iran
Key words: Lactoperoxidase, Enzyme stabilization, Gum tragacanth, Chitosan, nano biopolymer.
Lactoperoxidase (LPO) is a glycoprotein enzyme with a wide antimicrobial activity. Its stabilization is a key instrument for use LPO in industry. Gum tragacanth is a biopolymer, which is used for encapsulation and chitosan is used as a matrix for protein immobilization. This paper attempts to immobilize LPO by tragacanth-chitosan nano-biopolymers. Start with enzyme activity evaluating, LPO loading was done after analyzing tragacanth-chitosan nanocomposites by zeta sizer, FT-IR and SEM. Determining the nanocomposites proper size, the stability of immobilized and free LPO during storage was evaluated after 14 days of storage in 4 °C and 25 °C. Thermal stability also estimated by storing the immobilized and free LPO in different temperatures from 0 to 80 °C. It was found that, using nanocomposites with the size of 356.8 nm would result to preserving more stability during storage. The immobilized enzyme would have also more thermal stability. The results may be the consequences of encapsulation of LPO in tragacanth-chitosan nano-biopolymers. These findings suggest the application of tragacanth-chitosan nano-biopolymers in LPO immobilizing.