To obtain high currents, SWCNTs were used as nanoscaled electrical wires to facilitate DET between the CYTCDH of the native enzyme and the underlying electrode and to provide a large surface area for enzyme immobilization.
For DNA-based information storage, in which data are encoded in the transitions between bases rather than in their precise arrangement, the native enzyme and nucleotides can be used.
The turnover number of the adsorbed enzyme was determined as 28 ± 5 s−1 and is comparable to catalytic constant (36 ± 5 s−1) of the native enzyme in the solution.
However, the thermostability of the recombinant enzyme was better than the native enzyme.
CALGB 9511 used pegaspargase (PEG-ASP) in lieu of the native enzyme.
Thus the native enzyme appears to be a heterotrimer with a p63/p38/p35 (1:1:1) structure.
This suggests that the quaternary structure of the native enzyme is a dimer.
As a result, the immobilized ASNase II was more thermostable than the native enzyme.
In addition to this, the immobilization itself also leads to stabilization of the native enzyme structure.
The recombinant enzyme had similar specificity to the native enzyme, high affinity for 1-kestose, and low affinity for sucrose and inulin, although properties of the recombinant enzyme showed slight difference from those of the native one previously described.
