IMMOBILIZATION OF HORSODE PEROXIDASE BY TRAPPING AND COVALENT BONDING IN ALGINATE-PECTIN AND ALGINATE-PECTIN-STARCH HYBRID SUPPORT (Atena Editora)

Abstract

Horseradish peroxidase (HRP) is an enzyme with excellent biocatalytic activity and potential for industrial application. Aiming at large-scale applications, enzyme immobilization appears as an alternative for recovering and reusing enzymes, enabling employability and reducing costs. In this sense, the use of biopolymers has proven to be interesting, as they are non-toxic, biodegradable, renewable and highly available. However, there is still a lack of studies aimed at immobilizing HRP in hybrid biopolymers containing alginate, pectin and/or starch. Therefore, the present study aimed to immobilize HRP, through entrapment and covalent bonding, in alginate-pectin and alginate-pectin-starch granules, in addition to a control (alginate). For this, different gel compositions were prepared and extruded in calcium chloride solution using a syringe and needle (Ø = 1 mm). The granules were cross-linked by inserting them into a 0.02% glutaraldehyde solution. The parameters yield, efficiency and activity recovery were evaluated at time 0 h (initial) and after seven days of storage. The immobilization of HRP on alginate-pectin-starch granules proved to be superior in relation to alginate-pectin granules when evaluating the set of parameters, resulting in an activity recovery of 11.21% at time 0 h and 10.51% after seven days of storage. However, it is important to highlight that the control formulation (alginate), among all, showed the best recovery of activity after the storage period. Thus, in general, it can be concluded that the addition of pectin and/or starch in the composition of hybrid alginate gels has potential, however, further studies and optimizations are necessary.