Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran

• Published in: Molecules (Basel, Switzerland) Vol. 24; no. 20; p. 3648
• Main Authors: Wu, Zhuofu, Shi, Linjuan, Yu, Xiaoxiao, Zhang, Sitong, Chen, Guang
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 10-10-2019; MDPI
• Subjects: 2,5-diformylfuran; Catalase; Catalase - chemistry; co-immobilization; Decomposition; Dehydrogenases; Enzymes; Enzymes, Immobilized - chemistry; Furaldehyde - analogs & derivatives; Furaldehyde - chemistry; Furans - chemical synthesis; Galactose; Galactose oxidase; Glucose Oxidase - chemistry; Glycerol; Horseradish peroxidase; Horseradish Peroxidase - chemistry; Hydrogen peroxide; Hydroxymethylfurfural; Immobilization; Immobilized enzymes; Oxidation; Oxidation-Reduction; Peroxidase; Structure-function relationships; 2,5-diformylfuran; hydroxymethylfurfural; catalase; co-immobilization; galactose oxidase; horseradish peroxidase
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules24203648

Acting as a "green" manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural increases, the substrate causes oxidative damage to the activity of the tri-enzyme system, and the accumulated hydrogen peroxide produced by galactose oxidase causes tri-enzyme inactivation. The cost of tri-enzymes is also very high. These problems prevent the utilization of this enzyme toolbox in practice. To address this, galactose oxidase, catalase, and horseradish peroxidase were co-immobilized into Cu
(PO
)
nanoflowers in this study. The resulting co-immobilized tri-enzymes possessed better tolerance towards the oxidative damage caused by hydroxymethylfurfural at high concentrations, as compared to free tri-enzymes. Moreover, the 2,5-diformylfuran yield of co-immobilized tri-enzymes (95.7 ± 2.7%) was 1.06 times higher than that of separately immobilized enzymes (90.4 ± 1.9%). This result could be attributed to the boosted protective effect provided by catalase to the activity of galactose oxidase, owing to the physical proximity between them on the same support. After 30 recycles, co-immobilized tri-enzymes still achieves 86% of the initial yield. Moreover, co-immobilized tri-enzymes show enhanced thermal stability compared with free tri-enzymes. This work paves the way for the production of 2,5-diformylfuran from hydroxymethylfurfural via co-immobilized tri-enzymes.