Immobilization of trypsin on carbon

Concanavalin A Coated Activated Carbon for High Performance Enzymatic Catalysis

“…Finally, we compared above-mentioned two-step adsorption procedure against the cross-linking with glutaraldehyde, which has been extensively used for enzyme immobilization. ,, The cross-linked one shows a reusability around 90% after 10 cycles, which is comparable to 98% of laccase immobilized on ConA coated AC (Figure b). However, the cross-linking step led to a loss of laccase activity up to 55%.…”

“…Although physical adsorption is seemingly straightforward for enzyme immobilization, the surface force may lead to undesirable conformational changes and thus deactivation of the enzymes. , Moreover, the leakage of adsorbed enzymes prevents the practice of this idea. Chemical approaches such as cross-linking with glutaraldehyde, as described by Stoner and co-workers, and covalent binding with chemically modified AC, as described by Baily and co-workers, are effective in preventing enzyme leakage, the low activity caused by chemical treatment and harsh reaction conditions remain a major challenge hindering their practical applications. ,, …”

“…18,19 Moreover, the leakage of adsorbed enzymes prevents the practice of this idea. Chemical approaches such as cross-linking with glutaraldehyde, as described by Stoner and co-workers, 20 and covalent binding with chemically modified AC, as described by Baily 21 and co-workers, are effective in preventing enzyme leakage, the low activity caused by chemical treatment and harsh reaction conditions remain a major challenge hindering their practical applications. 1,22,23 Concanavalin A (ConA) is a type of lectin known for its capability to agglutinate glycoproteins through molecular recognition of carbohydrate containing nonreducing terminal α-D-mannosyl or α-D-glucosyl moieties.…”

Covalent linkage of glucose oxidase on modified glassy carbon electrodes. Kinetic phenomena

“…Hydrodynamic studies of rotating cylinder electrodes have shown that turbulent convection is occurring even at low rotation speeds. With the present experiments, where rotation speeds surpass 25 produced by the enzyme reaction as a function of working potential: ( ) 0.1 M glucose, 1.26 X -3 M oxygen; (•) 0.1 M glucose under nitrogen bubbling (presence of a small signal with high potential values is linked to oxygen produced by water oxidation); (A) Continuous work experiments were performed in the presence of 5 g L-1…”

Electropolymerized cobalt tetrakis(o-aminophenyl)porphyrin film mediated enzyme electrode for amperometric determination of glucose

“…The useful working range can be extended above these concentration limits by constructing calibration curves. Sir: In recent years, based on the recent, remarkable developments in the field of chemically modified electrodes (1, 2), immobilized enzyme chemically modified electrodes (IECMEs), which combine the specificity and selectivity of an enzyme for its natural substrate with the advantages of electrochemical detection, have become a research area of great interest (3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17). Enzymes are fixed onto electrode surfaces, generally by covalent attachment via intermediate linkages (e.g., using cyanuric chloride (3), glutaraldehyde (9)(10)(11)(12)18,19), carbodiimide (4-6), and boronate (20)). More recently, they are also entrapped in a polymer matrix electrochemically prepared on electrodes (14)(15)(16)(17).…”