کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1267864 | 972382 | 2015 | 11 صفحه PDF | دانلود رایگان |
• Laccase was immobilised on graphite functionalised by diazonium salt electroreduction.
• XPS and activity measurements were used to quantify laccase surface coverage.
• Coverage was four times higher for covalent grafting than for adsorption on the carboxylic surface.
• Oxidised laccase immobilisation increased the current density 5-times.
• The biocatalytic current with oxidised laccase reached 141 ± 37 μA cm− 2.
Graphite rods were modified by substituted aryldiazonium salts allowing subsequent laccase immobilisation and direct electron transfer at the cathode. Two covalent enzyme immobilisation methods were performed with carboxy and amino substituted grafted groups, either via the formation of an amide bond or a Schiff base between the glycosidic groups of the enzyme and the amino groups on the electrode surface, respectively. Laccase adsorption efficiency was consistently compared to the covalent attachment method on the same carbon surface, showing that the latter method led to a higher immobilisation yield when the electrode surface was functionalised with carboxylic groups, as shown from both laccase activity measurement towards an organic reducing substrate, ABTS, and quantitative XPS analysis. Both analytical methods led to similar laccase surface coverage estimations. From activity measurements, when laccase was covalently immobilised on the electrode functionalised with carboxylic groups, the surface coverage was found to be 43 ± 2% whereas it was only 10 ± 3% when laccase was adsorbed. Biocatalysed dioxygen reduction current was also higher in the case of covalent immobilisation. For the first time, oxidised laccase performances were compared to unmodified laccase, showing significant improved efficiency when using oxidised laccase: the current obtained with oxidised laccase was 141 ± 37 μA cm− 2 compared to 28 ± 6 μA cm− 2 for unmodified laccase after covalent immobilisation of the enzyme on a graphite electrode functionalised with carboxylic groups.
Journal: Bioelectrochemistry - Volume 106, Part A, December 2015, Pages 77–87