Valorization of Yacon ( <scp> <i>Smallanthus sonchifolius</i> </scp> ) peel for peroxidase production and its immobilization on alginate beads for 2,4‐dichlorophenol bioconversion

Abstract Yacon ( Smallanthus sonchifolius ) roots are emerging as an alternative source of peroxidase. This study aimed to extract, immobilize, and characterize the peroxidase from Yacon peel, herein designated as Yacon peel peroxidase (YPP), and apply it in the bioconversion of 2,4‐dichlorophenol. The alginate beads, both with and without immobilized YPP, were characterized by Brunauer–Emmett–Teller (BET), thermogravimetric analysis, scanning electron microscopy (SEM), and Fourier transform infrared spectroscopy (FTIR) analyses. The immobilized peroxidase showed maximum specific activity at 50°C and pH 13, using pyrogallol as a substrate. The reaction mechanism was identified as following a Ping‐Pong Bi‐Bi model. In the 2,4‐dichlorophenol bioconversion, the immobilized peroxidase showed maximum activity at 40°C, pH 6.8, and 0.5 mM H 2 O 2 after 360 min of reaction, achieving more than 80% of bioconversion. The biocatalyst was reused for four cycles, and its application in continuous reactors should be explored. Moreover, to assess the influence of the 2,4‐dichlorophenol molecules morphology and provide a better understanding of its bioconversion, density functional theory (DFT) was used to calculate chemical descriptors. The results suggest that immobilized Yacon peroxidase is a promising alternative for use in biocatalysis and the bioconversion of phenols.