Development of a glutamate-functionalized macroporous cation-exchange matrix for partial purification of lysozyme from chicken egg white

Abstract

The polymeric monoliths, called cryogels, arouse interest due to their versatility and to be a good alternative for enzyme purification processes. Lysozyme is an enzyme that stands out for its antimicrobial activity and is being used as a preservative in the food industry. This work aimed to produce a new cationic exchange matrix functionalized with monosodium glutamate for partial lysozyme purification of egg white. The structural characteristics of the support delivered were evaluated, presenting an ion exchange capacity (IEC) of 362×10−3 mol Na+. kg−1dry cryogel, zero charge point (PCZ) around pH 6.0, and porosity more significant than 90 %. The FTIR and TGA analyses proved that the modification of the XRD matrix indicated the material's amorphous nature. The hydrodynamic studies showed asymmetry, indicating the pores' non-uniformity and low resistance to flow. The lysozyme was purified from egg white, and a purification factor of 15.11 was obtained. SDS-PAGE electrophoresis analysis indicated high purity of lysozyme, with no other protein bands appearing in the eluted solution, indicating that the adsorbent has high potential for application in lysozyme purification processes.