Phenol Oxidase

Phenol oxidase is an enzyme which is responsible for hydroxylation of phenols and dehydrogenation of O. diphenols into quinone. It is known to be distributed in the blood as well as in the cuticle of crustaceans (Summers, 1967). The enzyme can be assayed either spectrophotometrically, by measuring the dopa chrome formed (Preston & Taylor, 1970) or monometrically by measuring the oxygen. consumed during the oxidation of the substrates (Hackman & Goldberg, 1967). The spectrophotometry method of assaying the enzyme of blood from Scylla serrata is presented here

High-Entropy Alloys as Catalysts for the CO2 and CO Reduction Reactions: Experimental Realization

Conversion of carbon dioxide into selective hydrocarbon using a stable catalyst remains a holy grail in the catalysis community. The high overpotential, stability, and selectivity in the use of a single-metal-based catalyst still remain a challenge. In current work, instead of using pure noble metals (Ag, Au, and Pt) as the catalyst, a nanocrystalline high-entropy alloy (HEA: AuAgPtPdCu) has been used for the conversion of CO2 into gaseous hydrocarbons. Utilizing an approach of multimetallic HEA, a faradic efficiency of about 100% toward gaseous products is obtained at a low applied potential (−0.3 V vs reversible hydrogen electrode). The reason behind the catalytic activity and selectivity of the high-entropy alloy (HEA) toward CO2 electroreduction was established through first-principles-based density functional theory (DFT) by comparing it with the pristine Cu(111) surface. This is attributed to the reversal in adsorption trends for two out of the total eight intermediates—*OCH3 and *O on Cu(111) and HEA surfaces

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Not AvailablePhenol oxidase is an enzyme which is responsible for hydroxylation of phenols and dehydrogenation of O. diphenols into quinone. It is known to be distributed in the blood as well as in the cuticle of crustaceans (Summers, 1967). The enzyme can be assayed either spectrophotometrically, by measuring the dopa chrome formed (Preston & Taylor, 1970) or monometrically by measuring the oxygen. consumed during the oxidation of the substrates (Hackman & Goldberg, 1967). The spectrophotometry method of assaying the enzyme of blood from Scylla serrata is presented here.Not Availabl

Formic acid and methanol electro-oxidation and counter hydrogen production using nano high entropy catalyst

Renewable harvesting of clean energy using the benefits of multi-metallic catalytic materials of high entropy alloy (HEA, equimolar CueAgeAuePtePd) from formic acid with minimum energy input has been achieved in the present investigation. The synergistic effect of pristine elements in the multimetallic HEA drives the electro-oxidation reaction towards non-carbonaceous pathway. The atomistic based simulations based on DFT rationalize the distinct lowering of the d-band center for the individual atoms in the HEA as compared to the pristine counterparts. Further this catalytic activity of the HEA has also been extended to methanol electro-oxidation to show the unique capability of the novel catalyst. The nanostructured HEA, prepared using a combination of casting and cryomilling techniques can further be utilized as the fuel cell anode in the direct formic acid/methanol fuel cells (DFFE)