AUTHOR=Zang Yuan-Yuan , Yang Sha , Xu Yong-Qiang , Chen Zhi-Gang , Wu Tao TITLE=Carrier-Free Immobilization of Rutin Degrading Enzyme Extracted From Fusarium spp. JOURNAL=Frontiers in Bioengineering and Biotechnology VOLUME=8 YEAR=2020 URL=https://www.frontiersin.org/journals/bioengineering-and-biotechnology/articles/10.3389/fbioe.2020.00470 DOI=10.3389/fbioe.2020.00470 ISSN=2296-4185 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.