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This chapter discusses extracellular matrix (ECM) proteins and ECM-derived peptides that might be immobilized on biomaterials, and surveys immobilization methodologies available for accomplishing this goal.
The influence of the immobilization methodologies on the electrochemical properties of the resulting surfaces was studied using hydroquinone and ferricyanide as redox probes.
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Functionalized graphene sheets were tailored and optimized as scaffold for α-amylase immobilization using Response Surface Methodology based on Box Behnken design, with an overall immobilization efficiency of 85.16%.
The second modification is the replacement of column-based cleanup with a Solid Phase Reversible Immobilization (SPRI) bead based methodology [ 33] as implemented by the Broad Institute [ 34].
Different methodologies employed for immobilization of bioreceptors on transducer surface and strategies for signal amplification will be discussed.
Therefore there remains a significant need for robust and simple methodologies for protein immobilization that can be applied to wide range of proteins and solid supports.
Based on response surface methodology, the optimal immobilization conditions obtained were: enzyme concentration, 2 mg/286 mg beads; optimal pH, 4.93; temperature, 28.88; cynuric chloride concentration, 0.17%; reaction time, 14.4 h, which resulted 74.51% maximum immobilization.
This study used the Box Behnken design and response surface methodology to optimize immobilization of Gluconobacter oxydans in Ca-alginate gel for the production of benzaldehyde in a biphasic system.
Optimizing parameters by Box-Behnken design of Response Surface Methodology, approximately 92% immobilization efficiency was achieved.
This reaction represents a rapid and green methodology for the polysaccharides immobilization on glass beads.
Optimization of the urease immobilization was carried using response surface methodology based on Central Composite Design.
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