Abstract
In this study, a strain with rutin degrading enzyme (RDE) activity was screened from moldy tartary buckwheat and subsequently identified as Fusarium spp. The structure and enzyme characteristics of CLEA-RDE formed by immobilization via cross-linking were then investigated. Further, the optimal catalysis conditions of CLEA-RDE in natural deep eutectic solvents (NADESs) serving as hydrolysis solvents were also investigated. The results of SEM and spectrum indicated that CLEA-RDE became more stable than free-RDE due to the cross-linking. Interestingly, CLEA-RDE showed a wider range of pH adaptation and higher tolerance to low temperatures (20 - 30°C) and hydrophobic environments. The results of orthogonal experiments revealed that the optimal condition for rutin hydrolysis was under pH 5.0 and 40oC with the degradation rate of 10.65 mg min-1 L-1. The preparation of CLEA-RDE without a carrier-based immobilization method reduces the loss of enzyme activity, improves the stability of the enzyme and can be applied to the investigation of immobilization of various enzymes, thus providing a referred idea for the improvement of catalysts in industrial production.