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At present, immobilization methods of DNA molecules include (1) chemical binding [ 55– 58], (2) physical stretching and binding [ 59, 60], and (3) electrical stretching and binding [ 25, 26, 61].
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If detergent and salt are simultaneously present during immobilization, a covalent attachment to the support is first produced.
We present the immobilization on synthetic substrates of elastin-like recombinamers (ELR) that combine a bioactive motif for cell adhesion with protein antifouling properties.
In the present electrochemical immobilization process, the coordinated Cu2+ ion is reduced (deposited) on an electrode surface electrochemically, and the deposited metal remains bounded to the objective molecule-tagged peptidic ligand on a solid (electrode) surface.
Herein, we present successful immobilization of the catalyst and efficient and selective conversion of butyraldehyde to butanol directly, without sacrificial electron-donor materials.
The results obtained by the xerogel entrapment method for the present LiP immobilization are comparable to those obtained by other methods such as the covalent bonding of the enzyme on siliceous cellular foams (McFs), Sepabeads EC-EP3 and Dilbeads NK supports or immobilization by the formation of cross-linked enzyme aggregates [ 9, 26].
In addition, the results obtained by the sol gel entrapment for the present MnP immobilization are superior to those reported for covalent binding of the enzyme on siliceous cellular foams, sepa beads and amine-terminated magnetic nano−composite by glutaraldehyde cross linking method [ 12, 13].
In addition, Schneider and Clark presented different immobilization strategies that have been used to create Cytochrome P450s (CYPs) biosensors, with particular emphasis on mammalian drug-metabolizing CYPs and characterization of CYP electrodes.
MnP isolated from solid-state culture of G. lucidum IBL-05, presented highest immobilization yield (83.9%%) using alginate beads prepared at optimized conditions of 4%% (w/v) sodium alginate, 2%% (w/v) Calcium chloride (CaCl2) and 0.5 mg/ml enzyme concentration.
In the present study an immobilization method in organic solvent was analyzed considering different immobilization parameters influencing the protein coupling and activity coupling.
Overall, the parametric model was stable if no hole or edge was present in the immobilization area.
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