2017
DOI: 10.1016/j.ijbiomac.2017.02.076
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Immobilization of laccase from Aspergillus oryzae on graphene nanosheets

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Cited by 75 publications
(18 citation statements)
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“…To research the effect of pH on the laccase immobilization, 10 mg support was put into 8 g/L laccase solutions with pH ranged from 3.0 to 7.0 at 25 ± 1 °C and contact time was 2 h. Generally, the strength of the acting force between the support and laccase during an adsorption process was decided by the charge properties of the support surface and the laccase molecule [26]. However, laccase enzyme shows different charge characteristics under different pH conditions, and the change of the electrostatic association will influence the recovered activity and laccase immobilization yield [27].…”
Section: Resultsmentioning
confidence: 99%
“…To research the effect of pH on the laccase immobilization, 10 mg support was put into 8 g/L laccase solutions with pH ranged from 3.0 to 7.0 at 25 ± 1 °C and contact time was 2 h. Generally, the strength of the acting force between the support and laccase during an adsorption process was decided by the charge properties of the support surface and the laccase molecule [26]. However, laccase enzyme shows different charge characteristics under different pH conditions, and the change of the electrostatic association will influence the recovered activity and laccase immobilization yield [27].…”
Section: Resultsmentioning
confidence: 99%
“…The structure of graphene-based nanomaterials can be an effective transducer since it allows the direct electron transfer between enzymes and electrodes [ 19 ]. Furthermore, graphene-based materials have been shown to be excellent substrates for increasing thermal stability, enzymatic activity, and for enzyme immobilization [ 105 107 ].…”
Section: Graphene-based Nanomaterials and Enzymesmentioning
confidence: 99%
“…The exceptional reusability of these biocatalytic systems is related to the stability and durability of the chitinous scaffolds [26] as well as the ability of this material to protect the immobilized enzyme against inactivation as a result of process conditions [85]. Furthermore, the enzyme-support interactions protect the enzyme against elution from the matrix, as tetracycline is washed out from the scaffolds between repeated uses [86]. Although the data show that the immobilized laccase is stable during repeated use, the decrease in tetracycline removal is related mainly to inactivation of the enzyme due to its inhibition by the macromolecular products of the reaction [87], although partial elution of the laccase from the support should not be excluded.…”
Section: Removal Of Tetracyclinementioning
confidence: 99%