EC Number   |
Application |
Reference |
|---|
   1.10.3.2 | analysis |
sensitive, rapid, and precise determination of phenols and their derivatives is important in environmental control and protection. An amperometric principle-based biosensor, employing immobilized laccase enzyme from Trametes versicolor, is developed for the detection of disubstituted methyl and methoxy phenols (industrial effluents). Evaluation of the influence of different enzyme immobilization techniques, on nylon membrane, on the performances of laccase-based Clark-type electrodes. The analytical properties and operating stabilities of the resulting biosensors are tested with different disubstituted methyl and methoxy derivatives of phenol substrates. Co-cross-linking method is superior to the other methods of immobilization in terms of sensitivity, limit of detection, response time, and operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent |
741797 |
| 1.10.3.2 | biofuel production |
construction of a long-life biofuel cell using a hyperthermophilic enzyme. For the cathode, the multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum is used, which catalyzes a four-electron reduction, and, for the anode, the PQQ-dependent glucose dehydrogenase from Pyrobaculum aerophilum is used. When the enzymes are used as electrodes, oriented with carbon nanotubes in a highly organized manner, the maximum output is 0.011 mW at 0.2 V. This output can be maintained 70% after 14 days |
-, 729480 |
| 1.10.3.2 | biofuel production |
lignin degradation of agricultural biomass for biofuel production |
746697 |
| 1.10.3.2 | biofuel production |
potential for bioconversion of lignin rich agricultural byproducts into animal feed and cellulosic ethanol. The enzyme effectively improves in vitro digestibility of maize straw |
743577 |
| 1.10.3.2 | biotechnology |
expression of non-fused enzyme and hydrophobin-enzyme fusion protein in Trichoderma reesei, intracellular accumulation and degradation of fusion protein, production of non-fused enzyme at up to 920 mg per l of fed-batch culture, purification from culture supernatant |
656736 |
| 1.10.3.2 | biotechnology |
five SvLAC genes (SvLAC9, SvLAC13, SvLAC15, SvLAC50, and SvLAC52) fulfill the criteria established to identify lignin-related candidates. They are strong candidates to be involved in lignin polymerization in Setaria viridis and might be good targets for lignin bioengineering strategies |
765630 |
| 1.10.3.2 | biotechnology |
robust catalytic efficiency in the presence of organic solvents suggest its industrial and biotechnological application potentials for the sustainable development of green chemistry |
764368 |
| 1.10.3.2 | biotechnology |
the purified enzyme displays greater efficiency in Remazol Brilliant Blue R decolourization (90%) in absence of redox mediator, an important property for biotechnological applications |
764870 |
| 1.10.3.2 | degradation |
bisphenol A degradation |
763996 |
| 1.10.3.2 | degradation |
cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. Due to phototrophic mode of nutrition, short generation time and easy mass cultivation, Spirulina platensis laccase appears as good candidate for laccase production. The high yield of laccase in short production period are profitable for its industrial application. Pure Spirulina platensis laccase alone can efficiently decolorized anthraquinonic dye Reactive Blue 4 without any mediators which makes it cost effective and suitable candidate for decolorization of synthetic dyes and help in waste water treatment |
-, 743619 |
