Synthesis of cross-linked protein-metal hybrid nanoflowers and its application in repeated batch decolorization of synthetic dyes

Patel, Sanjay; Otari, Sachin V.; Li, Jinglin; Kim, Dong Rip; Kim, Sun Chang; Cho, Byung-Kwan; Kalia, Vipin Chandra; Kang, Yun Chan; Lee, Jung-Kul

doi:10.1016/j.jhazmat.2018.01.003

Cited by 155 publications

(62 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Regarding the effect of organic solvents on the activity of immobilized enzymes, few studies were found, investigating their effect on the activity of lipases and laccases. In some cases, the immobilized enzymes showed higher activity levels than the free ones, but the results were variable, as observed as well in the present study 15,70,71…”

Section: Effect Of Potential Inhibitors and Activatorssupporting

confidence: 76%

Influence of Three Commercial Graphene Derivatives on the Catalytic Properties of a Lactobacillus plantarum α-l-Rhamnosidase When Used as Immobilization Matrices

Antón-Millán

García–Tojal

Marty-Roda

et al. 2018

ACS Appl. Mater. Interfaces

View full text Add to dashboard Cite

The modification of carbon nanomaterials with biological molecules paves the way toward their use in biomedical and biotechnological applications, such as next-generation biocatalytic processes, development of biosensors, implantable electronic devices, or drug delivery. In this study, different commercial graphene derivatives, namely, monolayer graphene oxide (GO), graphene oxide nanocolloids (GOCs), and polycarboxylate-functionalized graphene nanoplatelets (GNs), were compared as biomolecule carrier matrices. Detailed spectroscopic analyses showed that GO and GOC were similar in composition and functional group content and very different from GN, whereas divergent morphological characteristics were observed for each nanomaterial through microscopy analyses. The commercial α-l-rhamnosidase RhaB1 from the probiotic bacterium Lactobacillus plantarum, selected as a model biomolecule for its relevant role in the pharma and food industries, was directly immobilized on the different materials. The binding efficiency and biochemical properties of RhaB1-GO, RhaB1-GOC, and RhaB1-GN composites were analyzed. RhaB1-GO and RhaB1-GOC showed high binding efficiency, whereas the enzyme loading on GN, not tested in previous enzyme immobilization studies, was low. The enzyme showed contrasting changes when immobilized on the different material supports. The effect of pH on the activity of the three RhaB1-immobilized versions was similar to that observed for the free enzyme, whereas the activity-temperature profiles and the response to the presence of inhibitors varied significantly between the RhaB1 versions. In addition, the apparent K for the immobilized and soluble enzymes did not change. Finally, the free RhaB1 and the immobilized enzyme in GOC showed the best storage and reutilization stability, keeping most of their initial activity after 8 weeks of storage at 4 °C and 10 reutilization cycles, respectively. This study shows, for the first time, that distinct commercial graphene derivatives can influence differently the catalytic properties of an enzyme during its immobilization.

show abstract

Section: Effect Of Potential Inhibitors and Activatorssupporting

confidence: 76%

Influence of Three Commercial Graphene Derivatives on the Catalytic Properties of a Lactobacillus plantarum α-l-Rhamnosidase When Used as Immobilization Matrices

Antón-Millán

García–Tojal

Marty-Roda

et al. 2018

ACS Appl. Mater. Interfaces

View full text Add to dashboard Cite

show abstract

“…A C C E P T E D M A N U S C R I P T 4 as textile dye decolorization, pulp bleaching, detoxification and bioremediation of environmental pollutants and delignification or second generation ethanol production [2,4,5,6].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Purification and characterization of a fungal laccase from the ascomycete Thielavia sp. and its role in the decolorization of a recalcitrant dye

Mtibaà

Barriuso

Eugenio

et al. 2018

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

show abstract

“…It showed high oxidation potential (265% that of the free enzyme), and retained the residual enzyme efficiency of up to 84.6% under repeated batch conditions of 10 cycles [108] Chitosan crosslinked with genipin Improved pH, thermal, and storage stabilities of when compared with the free counterpart. The chitosan laccase system exhibited a residual activity of >55% after 11 cycles [109] polyacrylonitrile-biochar composite nanofibrous membrane High conversion for after 8 h of reaction [110] Table 3.…”

Section: Immobilization System Results Referencementioning

confidence: 97%

Dioxygen Activation by Laccases: Green Chemistry for Fine Chemical Synthesis

2018

View full text Add to dashboard Cite

Laccases are enzymes with attractive features for the synthesis of fine chemicals. The friendly reaction conditions of laccases and their high conversion and selectivity make them particularly suitable for green methods of synthesis. In addition, laccases are enzymes with broad substrate variability, ease of production, and no need of cofactors or aggressive oxidizing agents. Among molecules oxidized by laccases are polycyclic aromatic hydrocarbons, azo dyes, pesticides, phenols, and pharmaceuticals. This article reviews the laccase-mediated oxidation of fine chemicals for the production of biologically active compounds. The main aspects of the enzymatic oxidation are summarized; potentials and limitations are identified and proposals to develop more robust catalysts are analyzed.

show abstract

Synthesis of cross-linked protein-metal hybrid nanoflowers and its application in repeated batch decolorization of synthetic dyes

Cited by 155 publications

References 42 publications

Influence of Three Commercial Graphene Derivatives on the Catalytic Properties of a Lactobacillus plantarum α-l-Rhamnosidase When Used as Immobilization Matrices

Influence of Three Commercial Graphene Derivatives on the Catalytic Properties of a Lactobacillus plantarum α-l-Rhamnosidase When Used as Immobilization Matrices

Purification and characterization of a fungal laccase from the ascomycete Thielavia sp. and its role in the decolorization of a recalcitrant dye

Dioxygen Activation by Laccases: Green Chemistry for Fine Chemical Synthesis

Contact Info

Product

Resources

About