Multipoint immobilization and stabilization of amined peroxidases from soybean hull and chayote employing bacterial cellulose as support

Abstract

Peroxidases are homoproteins that catalyze redox processes, generating free radicals and polyaromatic products insoluble in water, facilitating their removal from the aqueous medium. The objective of this research was to extract the peroxidases of soybean and chayote, immobilize these enzymes on a highly activated bacterial cellulose (BC) support and use the derivatives obtained for discoloration of bromophenol blue. The amination of soluble peroxidases was realized in ethylenediamine buffer, at pH 4.75, and 10 and 50 mM carbodiimide. Amined peroxidases of 10 and 50 mM were covalently immobilized on the BC-glyoxyl support, with recovered activity of 82% for the derivative BC-Gly-S-NH2 50 mM and 92% for the derivative BC-Gly-Ch-NH2 50 mM. Total discoloration of bromophenol blue was obtained in 60 min, using the four amino derivatives. The derivatives were reused for five cycles and they maintained an average of 40% of their catalytic properties, suggesting that these products are suitable as a low-cost alternative for wastewater treatment and other industrial processes.