Biomedical Engineering Reference
In-Depth Information
Figure 7. Accumulation of TBI protein in the process of cultivation in a laboratory fermenter.
Table 1. The comparative characteristics of TBI protein isolated from biomass of
recombinant E.coli JM 103/pTBI strain
Cultivation
medium
Electrophoretic
purity, %
Yield of
TBI
protein, %
Pyrogenicity,
< 1.4 °C
LAL-
test, <25
EU/dose
Molecular
weight, kDa
YT
92
40
1.4
>45
20
TB plus
96
60
0.5
<25
20
Figures 6 and 7 show the growth curves of
E.coli
JM 103/pTBI and the content of the
TBI protein in biomass when cultured in a laboratory fermenter.
Finally, isolation of recombinant protein and its chromatographic purification were
carried out. Comparative qualitative and quantitative characteristics of TBI protein isolated in
the process of cultivation of
E.coli
JM 103/pTBI in TB plus and YT media are demonstrated
in Table 1.
It is seen that qualitative and quantitative characteristics of TBI protein isolated in the
process of cultivation of
E.coli
JM 103/pTBI in TB plus medium were better than those in YT
medium. When TB plus medium was used the yield of the target TBI protein was 60 % of its
initial content, with a purity of 96 % as compared to YT medium, in which the yield was 40
%, with a purity of 92 %.
C
ONCLUSION
1.
The optimal composition of the medium for cultivation of recombinant.
E.coli
JM
103/pTBI strain has been chosen. The content of the target protein was increased in
biomass by two-fold as compared to the control. The maximal yield of TBI protein
was in TB plus medium.
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