mesT demonstrated esterase as well as epoxide hydrolase activity. It was membrane bound and was upregulated under hypoxic conditions. The enzyme was able to degrade styrene oxide. The presence of antisense against this gene resulted in the inhibition of in vitro bacterial growth/survival in the presence of styrene oxide. Conclusion & future perspective: We demonstrated that mesT possessed epoxide hydrolase activity and styrene oxide might be its physiological substrate. Inhibition of mesT reduced the growth of the bacteria in presence of styrene oxide and its expression under hypoxic condition suggested its role in intracellular survival of bacteria.
mbtJ, an acetyl-hydrolase/esterase, enhanced the survival of M. tuberculosis under iron stress, affected the growth/infection efficiency in M. smegmatis, suggesting its pivotal role in the intracellular survival of bacterium.
is a natural blue colored protein of Spirulina platensis. Several methods based on chemical,
physical, and enzymatic processes have been reported for the extraction
of C-PC. However, most of the processes are either costly and/or time-consuming
and/or produce C-PC with less purity. In view of this, a very simple
and effective method was developed to extract C-PC with high purity
and without involving any energy-consuming process from S.
platensis. Wet biomass of S. platensis was
harvested and incubated in an optimized 2-(N-morpholino)ethanesulfonic
acid buffer with no supplement of any other compounds under dark,
anaerobic, and still conditions. These conditions facilitated the
leaching out of C-PC from the cells. The purity ratio of the blue
color C-PC supernatant obtained was enhanced by precipitation and
dialysis. The purity ratio of C-PC produced was 0.644 and increased
to 1.345 upon simple dialysis of the crude C-PC. The purity of C-PC
was 6.17 upon purifying through column chromatography. Hence, a simple
process was developed for producing C-PC of much higher purity than
therapeutic grade (>4). Furthermore, the molecular regulation of
extracellular release of C-PC from S. platensis cells
was monitored through relative expression levels of α and β
subunits of C-PC genes during specific buffer vis-à-vis water
as a control. Expression levels of genes encoding α and β
subunits of C-PC were found to be upregulated in the case of the 2-(N-morpholino)ethanesulfonic acid buffer treated algal cells
compared to water treated algal cells. The higher level expression
of these genes documented the higher and specific production of C-PC
by the S. platensis upon 2-(N-morpholino)ethanesulfonic
acid buffer treatment.
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