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Table 1 shows the maximum Q factors (Qmax) obtained with these substrates for each inductor design.
Electrolyte permeability with these substrates was also lower with higher pass speeds.
Soaking could have been one potential explanation for the higher bacterial attachment, but it is not the case with these substrates.
Further, the role of various catalysts such as Fe, Co, and Ni has also been extensively explored in conjunction with these substrates.
To clarify the mechanisms of hemicelluloses and pectin recognition and metabolism, we carried out a quantitative proteome analysis of C. cellulovorans cultured with these substrates.
Results found that OH reacted quickly with these substrates, with bimolecular reaction rate constants of 6.31 × 109, 5.13 × 109, and 7.05 × 109 M−1s−1 for 1-amantadine, 2-amantadine, and rimantadine, respectively.
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The chapter also discusses the unique strategies of the clostridia to cope with these substrate problems and highlights the features of some of the extracellular enzymes produced by these bacteria to degrade or hydrolyze biopolymers such as starch or cellulose.
The enantioselectivities of the acylase, which were evaluated with three of these substrates, were quite low (E values ranging between 1.9 and 7.2), but were significantly improved by substrate and/or solvent engineering.
In addition, resting cells of C. maltosa were incubated with dodecane-2-one, dodec-1-ene and dodecane after pre-cultivation with one of these substrates to show their conversion rates and the formation of products resulting from ketone degradation.
The enzyme follows Michaelis-Menten kinetics with respect to these substrates; KM values were 4, 620 in the presence of reduced glutathione and 380 μM in the presence of DTT.
We were unable to detect stable or specific interactions of Hhat with any of these substrates.
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