Amino-functionalized MOF immobilized laccase for enhancing enzyme activity stability and degrading Congo red

Li, Runze; Li, Xueping; Tian, Duoduo; Liu, Xiaochen; Wu, Zhansheng

doi:10.1016/j.jtice.2022.104647

Cited by 19 publications

(4 citation statements)

References 38 publications

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“…The immobilized enzyme retained 75.99% of its initial activity after 7 cycles. This finding is similar to the results of Li et al, who used hydrothermal synthesis of an amino-modified Cu MOF for the immobilized laccase degradation of Congo red dye. After 6 cycles, the degradation rate of Lac-Cu-MOF-NH 2 reached 84.63%, which notably improved the stability and activity of the enzyme.…”

Section: Resultssupporting

confidence: 91%

“…13 Moreover, MOFs can increase the enzyme load due to their unique properties. 14 To further exploit this potential, Zou et al 15 developed a bistable ZIF-8 through the ligand exchange mechanism. The newly constructed MOF exhibited a superior structural stability in aqueous and oil phases, and the immobilized enzyme molecule showed heightened conformational flexibility.…”

Section: Introductionmentioning

confidence: 99%

“…Metal–organic frameworks (MOFs) are widely used for their high specific surface area, adjustable and ultrahigh porosity, designable functionality, and good thermal stability . Moreover, MOFs can increase the enzyme load due to their unique properties . To further exploit this potential, Zou et al developed a bistable ZIF-8 through the ligand exchange mechanism.…”

Section: Introductionmentioning

confidence: 99%

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One-Step Purification and Immobilization of Glycosyltransferase with Zn–Ni MOF for the Synthesis of Rare Ginsenoside Rh2

Li,

Liu,

et al. 2024

ACS Appl. Mater. Interfaces

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Uridine diphosphate (UDP)-glucosyltransferases (UGTs) have received increasing attention in the field of ginsenoside Rh2 conversion. By harnessing the metal chelation between transition metal ions and imidazole groups present on Histagged enzymes, a specific immobilization of the enzyme within metal−organic frameworks (MOFs) is achieved. This innovative approach not only enhances the stability and reusability of the enzyme but also enables one-step purification and immobilization. Consequently, the need for purifying crude enzyme solutions is effectively circumvented, resulting in significant cost savings during experimentation. The use of immobilized enzymes in catalytic reactions has shown great potential for achieving higher conversion rates of ginsenoside Rh2. In this study, highly stable mesoporous Zn−Ni MOF materials were synthesized at 150 °C by a solvothermal method. The UGT immobilized on the Zn−Ni MOF (referred to as UGT@Zn−Ni MOF) exhibited superior pH adaptability and thermal stability, retaining approximately 76% of its initial activity even after undergoing 7 cycles. Furthermore, the relative activity of the immobilized enzyme remained at an impressive 80.22% even after 45 days of storage. The strong specific adsorption property of Zn−Ni MOF on His-tagged UGT was confirmed through analysis using polyacrylamide gel electrophoresis. UGT@Zn−Ni MOF was used to catalyze the conversion reaction, and the concentration of rare ginsenoside Rh2 was generated at 3.15 μg/mL. The results showed that Zn−Ni MOF is a material that can efficiently purify and immobilize His-tagged enzyme in one step and has great potential for industrial applications in enzyme purification and ginsenoside synthesis.

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Section: Resultssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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One-Step Purification and Immobilization of Glycosyltransferase with Zn–Ni MOF for the Synthesis of Rare Ginsenoside Rh2

Li,

Liu,

et al. 2024

ACS Appl. Mater. Interfaces

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“…Li et al used it to further fix Lac on the surface of Cu-MOF. The loading capacity was as high as 128.48 mg/g, and the activity was 2.57 times higher than that of the free enzyme activity [39]. Similarly, after enzyme crosslinking, immobilized Lac on aminated ZIF-8 could be used as green nano-biocatalysts for the treatment of industrial wastewater [40].…”

Section: Surface Immobilizationmentioning

confidence: 98%

Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives

Yang,

Zhang

et al. 2023

Materials

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Oxidoreductases are a wide class of enzymes that can catalyze biological oxidation and reduction reactions. Nowadays, oxidoreductases play a vital part in most bioenergetic metabolic pathways, which have important applications in biodegradation, bioremediation, environmental applications, as well as biosensors. However, free oxidoreductases are not stable and hard to be recycled. In addition, cofactors are needed in most oxidoreductases catalyze reactions, which are so expensive and unstable that it hinders their industrial applications. Enzyme immobilization is a feasible strategy that can overcome these problems. Recently, metal–organic frameworks (MOFs) have shown great potential as support materials for immobilizing enzymes due to their unique properties, such as high surface-area-to-volume ratio, chemical stability, functional designability, and tunable pore size. This review discussed the application of MOFs and their composites as immobilized carriers of oxidoreductase, as well as the application of MOFs as catalysts and immobilized carriers in redox reactions in the perspective of the function of MOFs materials. The paper also focuses on the potential of MOF carrier-based oxidoreductase immobilization for designing an enzyme cascade reaction system.

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Degradation of 2,4-DCP by immobilized laccase on modified biochar carrier

Xie,

Ren,

et al. 2023

Bioprocess Biosyst Eng

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Amino-functionalized MOF immobilized laccase for enhancing enzyme activity stability and degrading Congo red

Cited by 19 publications

References 38 publications

One-Step Purification and Immobilization of Glycosyltransferase with Zn–Ni MOF for the Synthesis of Rare Ginsenoside Rh2

One-Step Purification and Immobilization of Glycosyltransferase with Zn–Ni MOF for the Synthesis of Rare Ginsenoside Rh2

Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives

Degradation of 2,4-DCP by immobilized laccase on modified biochar carrier

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